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Delta-1-pyrroline-5-carboxylate synthase (P5CS) (Aldehyde dehydrogenase family 18 member A1) [Includes: Glutamate 5-kinase (GK) (EC 2.7.2.11) (Gamma-glutamyl kinase); Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)]

 P5CS_HUMAN              Reviewed;         795 AA.
P54886; B2R5Q4; B7Z350; B7Z5X8; B7ZLP1; D3DR44; O95952; Q3KQU2;
Q5T566; Q5T567; Q9UM72;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
20-JUN-2018, entry version 194.
RecName: Full=Delta-1-pyrroline-5-carboxylate synthase;
Short=P5CS;
AltName: Full=Aldehyde dehydrogenase family 18 member A1;
Includes:
RecName: Full=Glutamate 5-kinase;
Short=GK;
EC=2.7.2.11 {ECO:0000269|PubMed:26297558};
AltName: Full=Gamma-glutamyl kinase;
Includes:
RecName: Full=Gamma-glutamyl phosphate reductase;
Short=GPR;
EC=1.2.1.41 {ECO:0000269|PubMed:26297558};
AltName: Full=Glutamate-5-semialdehyde dehydrogenase;
AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase;
Name=ALDH18A1; Synonyms=GSAS, P5CS, PYCS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Kidney;
PubMed=8761662;
Aral B., Schlenzig J.S., Liu G., Kamoun P.;
"Database cloning human delta 1-pyrroline-5-carboxylate synthetase
(P5CS) cDNA: a bifunctional enzyme catalyzing the first 2 steps in
proline biosynthesis.";
C. R. Acad. Sci. III, Sci. Vie 319:171-178(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), FUNCTION, TISSUE
SPECIFICITY, AND ENZYME REGULATION (ISOFORMS LONG AND SHORT).
TISSUE=Small intestine;
PubMed=10037775; DOI=10.1074/jbc.274.10.6754;
Hu C.A., Lin W.-W., Obie C., Valle D.;
"Molecular enzymology of mammalian delta1-pyrroline-5-carboxylate
synthase. Alternative splice donor utilization generates isoforms with
different sensitivity to ornithine inhibition.";
J. Biol. Chem. 274:6754-6762(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), AND VARIANT
ILE-299.
TISSUE=Brain, and Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT), AND
VARIANTS ILE-299 AND TYR-372.
TISSUE=Brain, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
INVOLVEMENT IN ARCL3A, AND VARIANTS ARCL3A ARG-93 AND ILE-299.
PubMed=22170564; DOI=10.1007/s10545-011-9411-8;
Martinelli D., Haeberle J., Rubio V., Giunta C., Hausser I.,
Carrozzo R., Gougeard N., Marco-Marin C., Goffredo B.M.,
Meschini M.C., Bevivino E., Boenzi S., Colafati G.S., Brancati F.,
Baumgartner M.R., Dionisi-Vici C.;
"Understanding pyrroline-5-carboxylate synthetase deficiency:
clinical, molecular, functional, and expression studies, structure-
based analysis, and novel therapy with arginine.";
J. Inherit. Metab. Dis. 35:761-776(2012).
[9]
INVOLVEMENT IN ARCL3A, AND VARIANT ARCL3A CYS-782.
PubMed=24767728; DOI=10.1016/j.ejpn.2014.01.003;
Wolthuis D.F., van Asbeck E., Mohamed M., Gardeitchik T.,
Lim-Melia E.R., Wevers R.A., Morava E.;
"Cutis laxa, fat pads and retinopathy due to ALDH18A1 mutation and
review of the literature.";
Eur. J. Paediatr. Neurol. 18:511-515(2014).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INVOLVEMENT IN ADCL3,
VARIANTS ADCL3 GLN-138; LEU-138 AND TRP-138, AND CHARACTERIZATION OF
VARIANT ADCL3 TRP-138.
PubMed=26320891; DOI=10.1016/j.ajhg.2015.08.001;
Fischer-Zirnsak B., Escande-Beillard N., Ganesh J., Tan Y.X.,
Al Bughaili M., Lin A.E., Sahai I., Bahena P., Reichert S.L., Loh A.,
Wright G.D., Liu J., Rahikkala E., Pivnick E.K., Choudhri A.F.,
Krueger U., Zemojtel T., van Ravenswaaij-Arts C., Mostafavi R.,
Stolte-Dijkstra I., Symoens S., Pajunen L., Al-Gazali L.,
Meierhofer D., Robinson P.N., Mundlos S., Villarroel C.E., Byers P.,
Masri A., Robertson S.P., Schwarze U., Callewaert B., Reversade B.,
Kornak U.;
"Recurrent de novo mutations affecting residue Arg138 of pyrroline-5-
carboxylate synthase cause a progeroid form of autosomal-dominant
cutis laxa.";
Am. J. Hum. Genet. 97:483-492(2015).
[12]
INVOLVEMENT IN SPG9A, INVOLVEMENT IN SPG9B, VARIANTS SPG9A ALA-120;
GLN-252; PHE-652 AND LEU-665, AND VARIANTS SPG9B HIS-128; PRO-637 AND
HIS-715.
PubMed=26026163; DOI=10.1093/brain/awv143;
Coutelier M., Goizet C., Durr A., Habarou F., Morais S.,
Dionne-Laporte A., Tao F., Konop J., Stoll M., Charles P., Jacoupy M.,
Matusiak R., Alonso I., Tallaksen C., Mairey M., Kennerson M.,
Gaussen M., Schule R., Janin M., Morice-Picard F., Durand C.M.,
Depienne C., Calvas P., Coutinho P., Saudubray J.M., Rouleau G.,
Brice A., Nicholson G., Darios F., Loureiro J.L., Zuchner S.,
Ottolenghi C., Mochel F., Stevanin G.;
"Alteration of ornithine metabolism leads to dominant and recessive
hereditary spastic paraplegia.";
Brain 138:2191-2205(2015).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, SUBCELLULAR LOCATION,
INVOLVEMENT IN SPG9A, VARIANTS SPG9A LEU-243 AND GLN-252, AND
CHARACTERIZATION OF VARIANTS SPG9A LEU-243 AND GLN-252.
PubMed=26297558; DOI=10.1093/brain/awv247;
Panza E., Escamilla-Honrubia J.M., Marco-Marin C., Gougeard N.,
De Michele G., Morra V.B., Liguori R., Salviati L., Donati M.A.,
Cusano R., Pippucci T., Ravazzolo R., Nemeth A.H., Smithson S.,
Davies S., Hurst J.A., Bordo D., Rubio V., Seri M.;
"ALDH18A1 gene mutations cause dominant spastic paraplegia SPG9: loss
of function effect and plausibility of a dominant negative
mechanism.";
Brain 139:E3-E3(2016).
[15]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 362-795.
Structural genomics consortium (SGC);
"Crystal structure of human pyrroline-5-carboxylate synthetase.";
Submitted (JUL-2011) to the PDB data bank.
[16]
VARIANT ARCL3A GLN-84, CHARACTERIZATION OF VARIANT ARCL3A GLN-84,
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=11092761; DOI=10.1093/hmg/9.19.2853;
Baumgartner M.R., Hu C.A., Almashanu S., Steel G., Obie C., Aral B.,
Rabier D., Kamoun P., Saudubray J.-M., Valle D.;
"Hyperammonemia with reduced ornithine, citrulline, arginine and
proline: a new inborn error caused by a mutation in the gene encoding
delta(1)-pyrroline-5-carboxylate synthase.";
Hum. Mol. Genet. 9:2853-2858(2000).
[17]
VARIANT ARCL3A TYR-784, AND CHARACTERIZATION OF VARIANT ARCL3A
TYR-784.
PubMed=18478038; DOI=10.1038/ejhg.2008.91;
Bicknell L.S., Pitt J., Aftimos S., Ramadas R., Maw M.A.,
Robertson S.P.;
"A missense mutation in ALDH18A1, encoding Delta1-pyrroline-5-
carboxylate synthase (P5CS), causes an autosomal recessive
neurocutaneous syndrome.";
Eur. J. Hum. Genet. 16:1176-1186(2008).
-!- FUNCTION: Bifunctional enzyme that converts glutamate to glutamate
5-semialdehyde, an intermediate in the biosynthesis of proline,
ornithine and arginine. {ECO:0000269|PubMed:10037775,
ECO:0000269|PubMed:11092761, ECO:0000269|PubMed:26297558,
ECO:0000269|PubMed:26320891}.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5-
phosphate. {ECO:0000269|PubMed:26297558}.
-!- CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate +
NADP(+) = L-glutamyl 5-phosphate + NADPH.
{ECO:0000269|PubMed:26297558}.
-!- ENZYME REGULATION: Isoform Short: Inhibited by L-ornithine with a
Ki of approximately 0.25 mm. Isoform Long: Insensitive to
ornithine inhibition. This is due to the two amino acid insert
which abolishes feedback inhibition of P5CS activity by L-
ornithine. {ECO:0000269|PubMed:10037775}.
-!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
glutamate 5-semialdehyde from L-glutamate: step 1/2.
{ECO:0000269|PubMed:26297558}.
-!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
glutamate 5-semialdehyde from L-glutamate: step 2/2.
{ECO:0000269|PubMed:26297558}.
-!- SUBUNIT: Homohexamer or homotetramer.
{ECO:0000269|PubMed:26297558, ECO:0000269|PubMed:26320891}.
-!- INTERACTION:
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-1210304, EBI-741181;
Q96DZ9:CMTM5; NbExp=3; IntAct=EBI-1210304, EBI-2548702;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000269|PubMed:26297558, ECO:0000269|PubMed:26320891}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P54886-1; Sequence=Displayed;
Name=Short;
IsoId=P54886-2; Sequence=VSP_005215;
-!- DISEASE: Cutis laxa, autosomal recessive, 3A (ARCL3A)
[MIM:219150]: A syndrome characterized by facial dysmorphism with
a progeroid appearance, large and late-closing fontanel, cutis
laxa, joint hyperlaxity, athetoid movements and hyperreflexia,
pre- and postnatal growth retardation, intellectual deficit,
developmental delay, and ophthalmologic abnormalities.
{ECO:0000269|PubMed:11092761, ECO:0000269|PubMed:18478038,
ECO:0000269|PubMed:22170564, ECO:0000269|PubMed:24767728}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Cutis laxa, autosomal dominant, 3 (ADCL3) [MIM:616603]: A
form of cutis laxa, a connective tissue disorder characterized by
loose, hyperextensible skin with decreased resilience and
elasticity leading to a premature aged appearance. Face, hands,
feet, joints, and torso may be differentially affected. Additional
variable clinical features are gastrointestinal diverticula,
hernia, and genital prolapse. Rare manifestations are pulmonary
artery stenosis, aortic aneurysm, bronchiectasis, and emphysema.
ADCL3 patients manifest thin skin with visible veins and wrinkles,
cataract or corneal clouding, moderate intellectual disability,
muscular hypotonia with brisk muscle reflexes, clenched fingers,
and pre- and postnatal growth retardation.
{ECO:0000269|PubMed:26320891}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Spastic paraplegia 9A, autosomal dominant (SPG9A)
[MIM:601162]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. SPG9A patients have gait difficulties, motor neuropathy,
and dysarthria. Additional variable features include cerebellar
signs, cataract, pes cavus, and urinary urgency.
{ECO:0000269|PubMed:26026163, ECO:0000269|PubMed:26297558}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Spastic paraplegia 9B, autosomal recessive (SPG9B)
[MIM:616586]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. SPG9B is a complex form characterized by delayed
psychomotor development, intellectual disability, and severe motor
impairment. Dysmorphic facial features, tremor, and urinary
incontinence are variably observed in SPG9B patients.
{ECO:0000269|PubMed:26026163}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
kinase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the gamma-
glutamyl phosphate reductase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAH12086.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAH13064.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; X94453; CAA64224.1; -; mRNA.
EMBL; U76542; AAD17454.1; -; mRNA.
EMBL; U68758; AAD00169.1; -; mRNA.
EMBL; AK295487; BAH12086.1; ALT_INIT; mRNA.
EMBL; AK299557; BAH13064.1; ALT_INIT; mRNA.
EMBL; AK312271; BAG35201.1; -; mRNA.
EMBL; AL356632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49995.1; -; Genomic_DNA.
EMBL; CH471066; EAW49994.1; -; Genomic_DNA.
EMBL; CH471066; EAW49996.1; -; Genomic_DNA.
EMBL; CH471066; EAW49997.1; -; Genomic_DNA.
EMBL; BC106054; AAI06055.1; -; mRNA.
EMBL; BC117240; AAI17241.1; -; mRNA.
EMBL; BC117242; AAI17243.1; -; mRNA.
EMBL; BC143930; AAI43931.1; -; mRNA.
CCDS; CCDS31257.1; -. [P54886-2]
CCDS; CCDS7443.1; -. [P54886-1]
RefSeq; NP_001017423.1; NM_001017423.1. [P54886-2]
RefSeq; NP_001310341.1; NM_001323412.1.
RefSeq; NP_001310342.1; NM_001323413.1. [P54886-1]
RefSeq; NP_001310343.1; NM_001323414.1. [P54886-1]
RefSeq; NP_001310344.1; NM_001323415.1. [P54886-2]
RefSeq; NP_001310345.1; NM_001323416.1.
RefSeq; NP_001310348.1; NM_001323419.1.
RefSeq; NP_002851.2; NM_002860.3. [P54886-1]
UniGene; Hs.500645; -.
PDB; 2H5G; X-ray; 2.25 A; A/B=362-795.
PDBsum; 2H5G; -.
ProteinModelPortal; P54886; -.
SMR; P54886; -.
BioGrid; 111790; 42.
IntAct; P54886; 25.
MINT; P54886; -.
STRING; 9606.ENSP00000360268; -.
DrugBank; DB00142; L-Glutamic Acid.
iPTMnet; P54886; -.
PhosphoSitePlus; P54886; -.
SwissPalm; P54886; -.
BioMuta; ALDH18A1; -.
DMDM; 6226882; -.
EPD; P54886; -.
MaxQB; P54886; -.
PaxDb; P54886; -.
PeptideAtlas; P54886; -.
PRIDE; P54886; -.
ProteomicsDB; 56745; -.
ProteomicsDB; 56746; -. [P54886-2]
DNASU; 5832; -.
Ensembl; ENST00000371221; ENSP00000360265; ENSG00000059573. [P54886-2]
Ensembl; ENST00000371224; ENSP00000360268; ENSG00000059573. [P54886-1]
GeneID; 5832; -.
KEGG; hsa:5832; -.
UCSC; uc001kky.4; human. [P54886-1]
CTD; 5832; -.
DisGeNET; 5832; -.
EuPathDB; HostDB:ENSG00000059573.8; -.
GeneCards; ALDH18A1; -.
HGNC; HGNC:9722; ALDH18A1.
HPA; HPA008333; -.
HPA; HPA012604; -.
MalaCards; ALDH18A1; -.
MIM; 138250; gene.
MIM; 219150; phenotype.
MIM; 601162; phenotype.
MIM; 616586; phenotype.
MIM; 616603; phenotype.
neXtProt; NX_P54886; -.
OpenTargets; ENSG00000059573; -.
Orphanet; 35664; ALDH18A1-related De Barsy syndrome.
PharmGKB; PA34065; -.
eggNOG; KOG1154; Eukaryota.
eggNOG; KOG4165; Eukaryota.
eggNOG; COG0014; LUCA.
eggNOG; COG0263; LUCA.
GeneTree; ENSGT00500000044903; -.
HOVERGEN; HBG007911; -.
InParanoid; P54886; -.
KO; K12657; -.
OMA; MYVDSEA; -.
OrthoDB; EOG091G02MP; -.
PhylomeDB; P54886; -.
TreeFam; TF314372; -.
BioCyc; MetaCyc:HS00730-MONOMER; -.
Reactome; R-HSA-70614; Amino acid synthesis and interconversion (transamination).
UniPathway; UPA00098; UER00359.
UniPathway; UPA00098; UER00360.
ChiTaRS; ALDH18A1; human.
EvolutionaryTrace; P54886; -.
GeneWiki; Aldehyde_dehydrogenase_18_family,_member_A1; -.
GenomeRNAi; 5832; -.
PRO; PR:P54886; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000059573; -.
CleanEx; HS_ALDH18A1; -.
Genevisible; P54886; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017084; F:delta1-pyrroline-5-carboxylate synthetase activity; EXP:Reactome.
GO; GO:0004349; F:glutamate 5-kinase activity; IDA:UniProtKB.
GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0008652; P:cellular amino acid biosynthetic process; TAS:Reactome.
GO; GO:0019240; P:citrulline biosynthetic process; IMP:UniProtKB.
GO; GO:0006536; P:glutamate metabolic process; IMP:UniProtKB.
GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006592; P:ornithine biosynthetic process; IMP:UniProtKB.
GO; GO:0006561; P:proline biosynthetic process; IMP:UniProtKB.
CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
Gene3D; 3.40.1160.10; -; 1.
Gene3D; 3.40.309.10; -; 1.
Gene3D; 3.40.605.10; -; 2.
HAMAP; MF_00412; ProA; 1.
HAMAP; MF_00456; ProB; 1.
InterPro; IPR036393; AceGlu_kinase-like_sf.
InterPro; IPR016161; Ald_DH/histidinol_DH.
InterPro; IPR016163; Ald_DH_C.
InterPro; IPR016162; Ald_DH_N.
InterPro; IPR015590; Aldehyde_DH_dom.
InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
InterPro; IPR020593; G-glutamylP_reductase_CS.
InterPro; IPR001057; Glu/AcGlu_kinase.
InterPro; IPR005715; Glu_5kinase/COase_Synthase.
InterPro; IPR019797; Glutamate_5-kinase_CS.
InterPro; IPR000965; GPR_dom.
InterPro; IPR005766; P5_carboxy_syn.
Pfam; PF00696; AA_kinase; 1.
Pfam; PF00171; Aldedh; 1.
PIRSF; PIRSF036429; P5C_syn; 1.
PRINTS; PR00474; GLU5KINASE.
SUPFAM; SSF53633; SSF53633; 1.
SUPFAM; SSF53720; SSF53720; 1.
TIGRFAMs; TIGR01092; P5CS; 1.
TIGRFAMs; TIGR00407; proA; 1.
PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
PROSITE; PS01223; PROA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Amino-acid biosynthesis;
ATP-binding; Complete proteome; Disease mutation;
Hereditary spastic paraplegia; Kinase; Membrane; Mental retardation;
Mitochondrion; Mitochondrion inner membrane; Multifunctional enzyme;
NADP; Neurodegeneration; Nucleotide-binding; Oxidoreductase;
Polymorphism; Proline biosynthesis; Reference proteome; Transferase.
CHAIN 1 795 Delta-1-pyrroline-5-carboxylate synthase.
/FTId=PRO_0000109769.
NP_BIND 266 267 ATP. {ECO:0000250}.
NP_BIND 305 311 ATP. {ECO:0000250}.
REGION 1 361 Glutamate 5-kinase.
REGION 362 795 Gamma-glutamyl phosphate reductase.
BINDING 117 117 Substrate. {ECO:0000250}.
BINDING 223 223 Substrate. {ECO:0000250}.
BINDING 246 246 Substrate; via amide nitrogen.
{ECO:0000250}.
MOD_RES 311 311 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9Z110}.
MOD_RES 347 347 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9Z110}.
MOD_RES 550 550 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9Z110}.
VAR_SEQ 239 240 Missing (in isoform Short).
{ECO:0000303|PubMed:10037775,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005215.
VARIANT 84 84 R -> Q (in ARCL3A; reduction of activity;
dbSNP:rs121434582).
{ECO:0000269|PubMed:11092761}.
/FTId=VAR_038482.
VARIANT 93 93 G -> R (in ARCL3A).
{ECO:0000269|PubMed:22170564}.
/FTId=VAR_075884.
VARIANT 120 120 V -> A (in SPG9A; dbSNP:rs863224945).
{ECO:0000269|PubMed:26026163}.
/FTId=VAR_075885.
VARIANT 128 128 R -> H (in SPG9B; dbSNP:rs768323248).
{ECO:0000269|PubMed:26026163}.
/FTId=VAR_075886.
VARIANT 138 138 R -> L (in ADCL3; dbSNP:rs863225045).
{ECO:0000269|PubMed:26320891}.
/FTId=VAR_075887.
VARIANT 138 138 R -> Q (in ADCL3; dbSNP:rs863225045).
{ECO:0000269|PubMed:26320891}.
/FTId=VAR_075888.
VARIANT 138 138 R -> W (in ADCL3; no effect on protein
abundance; altered sub-mitochondrial
distribution; decreased proline
biosynthetic process; dbSNP:rs863225044).
{ECO:0000269|PubMed:26320891}.
/FTId=VAR_075889.
VARIANT 243 243 V -> L (in SPG9A; decreased protein
abundance; no effect on localization to
the mitochondrion; altered
homohexamerization; loss of glutamate 5-
kinase activity; no effect on glutamate-
5-semialdehyde dehydrogenase activity;
decreased amino acid biosynthetic
process; dbSNP:rs864321669).
{ECO:0000269|PubMed:26297558}.
/FTId=VAR_075890.
VARIANT 252 252 R -> Q (in SPG9A; altered
homohexamerization; no effect on
localization to the mitochondrion; loss
of glutamate 5-kinase activity; no effect
on glutamate-5-semialdehyde dehydrogenase
activity; decreased amino acid
biosynthetic process; dbSNP:rs864321670).
{ECO:0000269|PubMed:26026163,
ECO:0000269|PubMed:26297558}.
/FTId=VAR_075891.
VARIANT 299 299 T -> I (in ARCL3A; dbSNP:rs2275272).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:22170564}.
/FTId=VAR_051792.
VARIANT 372 372 S -> Y (in dbSNP:rs3765571).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_051793.
VARIANT 637 637 L -> P (in SPG9B; dbSNP:rs869320690).
{ECO:0000269|PubMed:26026163}.
/FTId=VAR_075892.
VARIANT 652 652 S -> F (in SPG9A).
{ECO:0000269|PubMed:26026163}.
/FTId=VAR_075893.
VARIANT 665 665 R -> L (in SPG9A; dbSNP:rs766264810).
{ECO:0000269|PubMed:26026163}.
/FTId=VAR_075894.
VARIANT 715 715 D -> H (in SPG9B; dbSNP:rs752669339).
{ECO:0000269|PubMed:26026163}.
/FTId=VAR_075895.
VARIANT 782 782 Y -> C (in ARCL3A; dbSNP:rs774047299).
{ECO:0000269|PubMed:24767728}.
/FTId=VAR_075896.
VARIANT 784 784 H -> Y (in ARCL3A; does not affect
proline and ornithine biosynthetic
activity; dbSNP:rs121434583).
{ECO:0000269|PubMed:18478038}.
/FTId=VAR_058006.
CONFLICT 87 87 E -> K (in Ref. 3; BAG35201).
{ECO:0000305}.
CONFLICT 126 126 R -> T (in Ref. 1; CAA64224).
{ECO:0000305}.
CONFLICT 266 266 S -> P (in Ref. 1; CAA64224).
{ECO:0000305}.
CONFLICT 299 299 T -> P (in Ref. 1; CAA64224).
{ECO:0000305}.
CONFLICT 305 307 MGG -> NGC (in Ref. 1; CAA64224).
{ECO:0000305}.
CONFLICT 314 315 AA -> ST (in Ref. 1; CAA64224).
{ECO:0000305}.
CONFLICT 487 493 LPQVAAL -> PTPGGSF (in Ref. 1; CAA64224).
{ECO:0000305}.
HELIX 363 379 {ECO:0000244|PDB:2H5G}.
HELIX 382 398 {ECO:0000244|PDB:2H5G}.
HELIX 400 414 {ECO:0000244|PDB:2H5G}.
TURN 415 417 {ECO:0000244|PDB:2H5G}.
HELIX 420 424 {ECO:0000244|PDB:2H5G}.
HELIX 430 446 {ECO:0000244|PDB:2H5G}.
STRAND 454 461 {ECO:0000244|PDB:2H5G}.
STRAND 464 472 {ECO:0000244|PDB:2H5G}.
STRAND 475 482 {ECO:0000244|PDB:2H5G}.
HELIX 486 497 {ECO:0000244|PDB:2H5G}.
STRAND 500 504 {ECO:0000244|PDB:2H5G}.
HELIX 507 509 {ECO:0000244|PDB:2H5G}.
HELIX 510 525 {ECO:0000244|PDB:2H5G}.
TURN 526 528 {ECO:0000244|PDB:2H5G}.
HELIX 530 532 {ECO:0000244|PDB:2H5G}.
STRAND 533 535 {ECO:0000244|PDB:2H5G}.
STRAND 553 559 {ECO:0000244|PDB:2H5G}.
HELIX 561 570 {ECO:0000244|PDB:2H5G}.
STRAND 572 574 {ECO:0000244|PDB:2H5G}.
STRAND 584 588 {ECO:0000244|PDB:2H5G}.
TURN 594 596 {ECO:0000244|PDB:2H5G}.
HELIX 597 606 {ECO:0000244|PDB:2H5G}.
STRAND 614 621 {ECO:0000244|PDB:2H5G}.
HELIX 622 624 {ECO:0000244|PDB:2H5G}.
HELIX 628 639 {ECO:0000244|PDB:2H5G}.
STRAND 643 646 {ECO:0000244|PDB:2H5G}.
HELIX 648 651 {ECO:0000244|PDB:2H5G}.
STRAND 670 680 {ECO:0000244|PDB:2H5G}.
HELIX 681 691 {ECO:0000244|PDB:2H5G}.
STRAND 694 700 {ECO:0000244|PDB:2H5G}.
HELIX 704 713 {ECO:0000244|PDB:2H5G}.
STRAND 716 723 {ECO:0000244|PDB:2H5G}.
HELIX 725 727 {ECO:0000244|PDB:2H5G}.
TURN 730 734 {ECO:0000244|PDB:2H5G}.
STRAND 745 747 {ECO:0000244|PDB:2H5G}.
HELIX 754 757 {ECO:0000244|PDB:2H5G}.
STRAND 758 765 {ECO:0000244|PDB:2H5G}.
HELIX 771 774 {ECO:0000244|PDB:2H5G}.
SEQUENCE 795 AA; 87302 MW; 8BF27EF2A8FB2D79 CRC64;
MLSQVYRCGF QPFNQHLLPW VKCTTVFRSH CIQPSVIRHV RSWSNIPFIT VPLSRTHGKS
FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE QVSVLQNQGR EMMLVTSGAV
AFGKQRLRHE ILLSQSVRQA LHSGQNQLKE MAIPVLEARA CAAAGQSGLM ALYEAMFTQY
SICAAQILVT NLDFHDEQKR RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV
ISVKDNDSLA ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK
SRVGMGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG TFFSEVKPAG
PTVEQQGEMA RSGGRMLATL EPEQRAEIIH HLADLLTDQR DEILLANKKD LEEAEGRLAA
PLLKRLSLST SKLNSLAIGL RQIAASSQDS VGRVLRRTRI AKNLELEQVT VPIGVLLVIF
ESRPDCLPQV AALAIASGNG LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAVQLVNTRE
EVEDLCRLDK MIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL
VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF ASYLTFSPSE
VKSLRTEYGD LELCIEVVDN VQDAIDHIHK YGSSHTDVIV TEDENTAEFF LQHVDSACVF
WNASTRFSDG YRFGLGAEVG ISTSRIHARG PVGLEGLLTT KWLLRGKDHV VSDFSEHGSL
KYLHENLPIP QRNTN


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