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Protein arg11, mitochondrial [Cleaved into: N-acetyl-gamma-glutamyl-phosphate reductase (EC 1.2.1.38) (N-acetyl-glutamate semialdehyde dehydrogenase) (NAGSA dehydrogenase); Acetylglutamate kinase (EC 2.7.2.8) (N-acetyl-L-glutamate 5-phosphotransferase) (NAG kinase) (AGK)]

 ARG56_SCHPO             Reviewed;         885 AA.
P31318;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
25-OCT-2017, entry version 148.
RecName: Full=Protein arg11, mitochondrial;
Contains:
RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase;
EC=1.2.1.38;
AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase;
Short=NAGSA dehydrogenase;
Contains:
RecName: Full=Acetylglutamate kinase;
EC=2.7.2.8;
AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase;
AltName: Full=NAG kinase;
Short=AGK;
Flags: Precursor;
Name=arg11; ORFNames=SPAC4G9.09c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 38365 / 975;
PubMed=1313366; DOI=10.1111/j.1432-1033.1992.tb16749.x;
van Huffel C., Dubois E., Messenguy F.;
"Cloning and sequencing of arg3 and arg11 genes of Schizosaccharomyces
pombe on a 10-kb DNA fragment. Heterologous expression and
mitochondrial targeting of their translation products.";
Eur. J. Biochem. 205:33-43(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
-!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+)
+ phosphate = N-acetyl-5-glutamyl phosphate + NADPH.
-!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-
glutamate 5-phosphate.
-!- ENZYME REGULATION: The kinase activity is inhibited by arginine.
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
acetyl-L-ornithine from L-glutamate: step 2/4.
-!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-
acetyl-L-ornithine from L-glutamate: step 3/4.
-!- SUBCELLULAR LOCATION: Mitochondrion.
-!- PTM: The protein precursor is cleaved into the two biologically
active enzymes, the kinase and the reductase.
-!- SIMILARITY: In the N-terminal section; belongs to the
acetylglutamate kinase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the NAGSA
dehydrogenase family. {ECO:0000305}.
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EMBL; X63576; CAA45132.1; -; Genomic_DNA.
EMBL; CU329670; CAA93559.1; -; Genomic_DNA.
PIR; S22389; S22389.
RefSeq; NP_593691.1; NM_001019123.2.
ProteinModelPortal; P31318; -.
SMR; P31318; -.
BioGrid; 279813; 44.
MINT; MINT-4688310; -.
STRING; 4896.SPAC4G9.09c.1; -.
iPTMnet; P31318; -.
MaxQB; P31318; -.
PRIDE; P31318; -.
EnsemblFungi; SPAC4G9.09c.1; SPAC4G9.09c.1:pep; SPAC4G9.09c.
GeneID; 2543391; -.
KEGG; spo:SPAC4G9.09c; -.
EuPathDB; FungiDB:SPAC4G9.09c; -.
PomBase; SPAC4G9.09c; arg11.
HOGENOM; HOG000201928; -.
InParanoid; P31318; -.
KO; K12659; -.
OMA; DENRAWH; -.
OrthoDB; EOG092C2W4A; -.
PhylomeDB; P31318; -.
UniPathway; UPA00068; UER00107.
UniPathway; UPA00068; UER00108.
PRO; PR:P31318; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0005759; C:mitochondrial matrix; IDA:PomBase.
GO; GO:0005739; C:mitochondrion; IDA:PomBase.
GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central.
GO; GO:0003991; F:acetylglutamate kinase activity; IGI:PomBase.
GO; GO:0034618; F:arginine binding; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IMP:PomBase.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0006526; P:arginine biosynthetic process; IMP:PomBase.
GO; GO:0006592; P:ornithine biosynthetic process; ISS:PomBase.
Gene3D; 3.40.1160.10; -; 1.
HAMAP; MF_00150; ArgC_type1; 1.
InterPro; IPR036393; AceGlu_kinase-like_sf.
InterPro; IPR004662; AcgluKinase.
InterPro; IPR023013; AGPR_AS.
InterPro; IPR000706; AGPR_type-1.
InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR011241; NAGK/NAGSA.
InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
InterPro; IPR006855; Vertebrate-like_GNAT_dom.
Pfam; PF00696; AA_kinase; 1.
Pfam; PF04768; NAT; 1.
Pfam; PF01118; Semialdhyde_dh; 1.
PIRSF; PIRSF036440; ARG5-6; 1.
SMART; SM00859; Semialdhyde_dh; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF53633; SSF53633; 1.
TIGRFAMs; TIGR00761; argB; 1.
TIGRFAMs; TIGR01850; argC; 1.
PROSITE; PS01224; ARGC; 1.
PROSITE; PS51731; GNAT_NAGS; 1.
3: Inferred from homology;
Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
Cleavage on pair of basic residues; Complete proteome; Kinase;
Mitochondrion; Multifunctional enzyme; NADP; Nucleotide-binding;
Oxidoreductase; Reference proteome; Transferase; Transit peptide.
TRANSIT 1 59 Mitochondrion. {ECO:0000255}.
CHAIN 60 550 Acetylglutamate kinase. {ECO:0000255}.
/FTId=PRO_0000002071.
CHAIN 551 885 N-acetyl-gamma-glutamyl-phosphate
reductase. {ECO:0000255}.
/FTId=PRO_0000002072.
DOMAIN 346 499 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
ACT_SITE 703 703 {ECO:0000255|PROSITE-ProRule:PRU10010}.
VARIANT 261 261 V -> D (in strain: 975).
VARIANT 345 345 G -> P (in strain: 975).
SEQUENCE 885 AA; 97705 MW; 3AA1A5082431B118 CRC64;
MLIELQQIVK SGLVRNGAKH CTKRSLLCSN ASVIASKRFQ GSFAPGQQQP LNPLAKPIEQ
DRDAIIRILS SIGSRREVEQ YLRYFTSFEA QRFAIIKVGG AIITDELDTL AQSLAFLNHV
GLYPIVVHGA GPQLNKILAS RNVEPEYSDG IRITDAETLS VARKVFLEEN AKLVDALEKL
GTRARPITGG VFQAEYLDKE KYKYVGKIVK VNKAPIEHSI RAGTLPILTS MAETASGQLL
NVNADITAGE LARVLKPLKV VYLNEKGGLI NGETKKKISS IYLDREYDGL MKQPWVKYGT
KLKIKEIKEL LDTLPRTSSV AIISTKDLQK ELFTESGAGT LISRGFVINK HDSLDSIPDA
ALENLIIQKN SLAAPSESLK QFKDTLKDRK LRIYSDSFNE SVAIVDTTDS SLPVLLAFGA
ADNNWLNNVV DSILTTLKAD FPSLLWRLQP SAKNLEWFFS KSEGTLFANN FYYFWYGVKD
LNKISKFIQS DKPFADAIIQ TQSTKPPTAS STTNNPSSSQ INQKRSYSTS SLFSKNKKMN
RSLFLKGGKR FFSAEAQKTQ KPLKAVSSKP AKVVLLGARG YTGKNLIGLI NTHPYLELSH
VSSRELEGTK LPGYTKKEIQ YVNLSTDDVK KLEEEGAVDA WVMALPNGVC KPYVDALTSA
NGKSVIVDLS ADYRFEPSWQ YGLPELNDRE ALRNSKRISN PGCYATGSQV GLTPILSLID
GQPSIFGVSG YSGAGTKPSP KNDLNVLTNN LIPYSLTDHI HEREISYRLK QPVAFIPHVA
QWFQGITLTI NVPLKKSITS RELRNLYQDR YNGEPLIHVQ GDVPLVKDNA HKHHVSVGGF
GVHSSGKRAV IVVTIDNLLK GAATQALQNL NLSCGYDEYA GIHLD


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