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Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC 6.2.1.4) (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha)

 SUCA_HUMAN              Reviewed;         346 AA.
P53597; Q9BWB0; Q9UNP6;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 4.
12-SEP-2018, entry version 187.
RecName: Full=Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222};
EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03222};
EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03222};
AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03222};
Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_03222};
Flags: Precursor;
Name=SUCLG1 {ECO:0000255|HAMAP-Rule:MF_03222};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-346.
TISSUE=Lung;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-346.
Tews K.N., Mehus J.G., Johnson J.D., Milavetz B.I., Lambeth D.O.;
"Sequence of the alpha subunit of succinyl-CoA synthetase in human.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-145.
TISSUE=Brain, and Skeletal muscle;
PubMed=9128182; DOI=10.1016/S0925-4439(96)00076-2;
James M., Man N.T., Edwards Y.H., Morris G.E.;
"The molecular basis for cross-reaction anti-dystrophin antibody with
alpha-actinin.";
Biochim. Biophys. Acta 1360:169-176(1997).
[5]
INVOLVEMENT IN MTDPS9.
PubMed=17668387; DOI=10.1086/519222;
Ostergaard E., Christensen E., Kristensen E., Mogensen B., Duno M.,
Shoubridge E.A., Wibrand F.;
"Deficiency of the alpha subunit of succinate-coenzyme A ligase causes
fatal infantile lactic acidosis with mitochondrial DNA depletion.";
Am. J. Hum. Genet. 81:383-387(2007).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[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]
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).
[9]
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).
[10]
VARIANT MTDPS9 ALA-85.
PubMed=19526370; DOI=10.1007/s00431-009-1007-z;
Ostergaard E., Schwartz M., Batbayli M., Christensen E.,
Hjalmarson O., Kollberg G., Holme E.;
"A novel missense mutation in SUCLG1 associated with mitochondrial DNA
depletion, encephalomyopathic form, with methylmalonic aciduria.";
Eur. J. Pediatr. 169:201-205(2010).
[11]
VARIANT MTDPS9 ARG-170.
PubMed=20693550; DOI=10.1136/jmg.2009.073445;
Rouzier C., Le Guedard-Mereuze S., Fragaki K., Serre V., Miro J.,
Tuffery-Giraud S., Chaussenot A., Bannwarth S., Caruba C.,
Ostergaard E., Pellissier J.F., Richelme C., Espil C., Chabrol B.,
Paquis-Flucklinger V.;
"The severity of phenotype linked to SUCLG1 mutations could be
correlated with residual amount of SUCLG1 protein.";
J. Med. Genet. 47:670-676(2010).
[12]
VARIANT MTDPS9 LEU-14.
PubMed=20453710; DOI=10.1203/PDR.0b013e3181e5c3a4;
Van Hove J.L., Saenz M.S., Thomas J.A., Gallagher R.C., Lovell M.A.,
Fenton L.Z., Shanske S., Myers S.M., Wanders R.J., Ruiter J.,
Turkenburg M., Waterham H.R.;
"Succinyl-CoA ligase deficiency: a mitochondrial
hepatoencephalomyopathy.";
Pediatr. Res. 68:159-164(2010).
[13]
VARIANT ALA-37.
PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
"Homozygous missense mutation in the LMAN2L gene segregates with
intellectual disability in a large consanguineous Pakistani family.";
J. Med. Genet. 53:138-144(2016).
-!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid
cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
synthesis of either ATP or GTP and thus represents the only step
of substrate-level phosphorylation in the TCA. The alpha subunit
of the enzyme binds the substrates coenzyme A and phosphate, while
succinate binding and specificity for either ATP or GTP is
provided by different beta subunits. {ECO:0000255|HAMAP-
Rule:MF_03222}.
-!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_03222}.
-!- CATALYTIC ACTIVITY: GTP + succinate + CoA = GDP + phosphate +
succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_03222}.
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
succinate from succinyl-CoA (ligase route): step 1/1.
{ECO:0000255|HAMAP-Rule:MF_03222}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Different
beta subunits determine nucleotide specificity. Together with the
ATP-specific beta subunit SUCLA2, forms an ADP-forming succinyl-
CoA synthetase (A-SCS). Together with the GTP-specific beta
subunit SUCLG2 forms a GDP-forming succinyl-CoA synthetase (G-
SCS). {ECO:0000255|HAMAP-Rule:MF_03222}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-
Rule:MF_03222}.
-!- DISEASE: Mitochondrial DNA depletion syndrome 9 (MTDPS9)
[MIM:245400]: A severe disorder due to mitochondrial dysfunction.
It is characterized by infantile onset of hypotonia, lactic
acidosis, severe psychomotor retardation, progressive neurologic
deterioration, and excretion of methylmalonic acid.
{ECO:0000269|PubMed:17668387, ECO:0000269|PubMed:19526370,
ECO:0000269|PubMed:20453710, ECO:0000269|PubMed:20693550}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha
subunit family. {ECO:0000255|HAMAP-Rule:MF_03222}.
-!- SEQUENCE CAUTION:
Sequence=AAD17940.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH00504.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA92426.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AC096770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000504; AAH00504.1; ALT_INIT; mRNA.
EMBL; AF104921; AAD17940.2; ALT_INIT; mRNA.
EMBL; Z68204; CAA92426.1; ALT_INIT; mRNA.
CCDS; CCDS1967.2; -.
RefSeq; NP_003840.2; NM_003849.3.
UniGene; Hs.270428; -.
PDB; 6G4Q; X-ray; 2.59 A; A=42-346.
PDBsum; 6G4Q; -.
ProteinModelPortal; P53597; -.
SMR; P53597; -.
BioGrid; 114330; 20.
CORUM; P53597; -.
IntAct; P53597; 9.
MINT; P53597; -.
STRING; 9606.ENSP00000377446; -.
DrugBank; DB00139; Succinic acid.
iPTMnet; P53597; -.
PhosphoSitePlus; P53597; -.
BioMuta; SUCLG1; -.
DMDM; 223634731; -.
UCD-2DPAGE; P53597; -.
EPD; P53597; -.
MaxQB; P53597; -.
PaxDb; P53597; -.
PeptideAtlas; P53597; -.
PRIDE; P53597; -.
ProteomicsDB; 56587; -.
TopDownProteomics; P53597; -.
Ensembl; ENST00000393868; ENSP00000377446; ENSG00000163541.
GeneID; 8802; -.
KEGG; hsa:8802; -.
UCSC; uc002son.4; human.
CTD; 8802; -.
DisGeNET; 8802; -.
EuPathDB; HostDB:ENSG00000163541.11; -.
GeneCards; SUCLG1; -.
HGNC; HGNC:11449; SUCLG1.
HPA; HPA036683; -.
HPA; HPA036684; -.
MalaCards; SUCLG1; -.
MIM; 245400; phenotype.
MIM; 611224; gene.
neXtProt; NX_P53597; -.
OpenTargets; ENSG00000163541; -.
Orphanet; 17; Fatal infantile lactic acidosis with methylmalonic aciduria.
PharmGKB; PA36246; -.
eggNOG; KOG1255; Eukaryota.
eggNOG; COG0074; LUCA.
GeneTree; ENSGT00530000063275; -.
HOGENOM; HOG000239685; -.
HOVERGEN; HBG000957; -.
InParanoid; P53597; -.
KO; K01899; -.
OMA; IIFVPPA; -.
OrthoDB; EOG091G0D9C; -.
PhylomeDB; P53597; -.
TreeFam; TF300666; -.
BioCyc; MetaCyc:HS08877-MONOMER; -.
BRENDA; 6.2.1.4; 2681.
BRENDA; 6.2.1.5; 2681.
Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
UniPathway; UPA00223; UER00999.
ChiTaRS; SUCLG1; human.
GeneWiki; SUCLG1; -.
GenomeRNAi; 8802; -.
PRO; PR:P53597; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163541; Expressed in 231 organ(s), highest expression level in cortex of kidney.
CleanEx; HS_SUCLG1; -.
ExpressionAtlas; P53597; baseline and differential.
Genevisible; P53597; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0048037; F:cofactor binding; IEA:InterPro.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IBA:GO_Central.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.261; -; 1.
HAMAP; MF_01988; Succ_CoA_alpha; 1.
InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
InterPro; IPR003781; CoA-bd.
InterPro; IPR005810; CoA_lig_alpha.
InterPro; IPR005811; CoA_ligase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR016102; Succinyl-CoA_synth-like.
Pfam; PF02629; CoA_binding; 1.
Pfam; PF00549; Ligase_CoA; 1.
PIRSF; PIRSF001553; SucCS_alpha; 1.
SMART; SM00881; CoA_binding; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF52210; SSF52210; 1.
TIGRFAMs; TIGR01019; sucCoAalpha; 1.
PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Disease mutation;
Ligase; Mitochondrion; Nucleotide-binding; Polymorphism;
Primary mitochondrial disease; Reference proteome; Transit peptide;
Tricarboxylic acid cycle.
TRANSIT 1 40 Mitochondrion. {ECO:0000250}.
CHAIN 41 346 Succinate--CoA ligase [ADP/GDP-forming]
subunit alpha, mitochondrial.
/FTId=PRO_0000033340.
REGION 64 67 Coenzyme A binding. {ECO:0000255|HAMAP-
Rule:MF_03222}.
REGION 143 145 Coenzyme A binding. {ECO:0000255|HAMAP-
Rule:MF_03222}.
ACT_SITE 299 299 Tele-phosphohistidine intermediate.
{ECO:0000255|HAMAP-Rule:MF_03222}.
BINDING 90 90 Coenzyme A. {ECO:0000255|HAMAP-
Rule:MF_03222}.
BINDING 207 207 Substrate; shared with subunit beta.
{ECO:0000255|HAMAP-Rule:MF_03222}.
MOD_RES 54 54 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 57 57 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9WUM5}.
MOD_RES 57 57 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9WUM5}.
MOD_RES 66 66 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q9WUM5}.
MOD_RES 66 66 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q9WUM5}.
MOD_RES 81 81 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9WUM5}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9WUM5}.
MOD_RES 338 338 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9WUM5}.
VARIANT 14 14 M -> L (in MTDPS9; with progressive liver
disease and recurrent hepatic failure).
{ECO:0000269|PubMed:20453710}.
/FTId=VAR_065120.
VARIANT 37 37 G -> A (in dbSNP:rs369610897).
{ECO:0000269|PubMed:26566883}.
/FTId=VAR_076432.
VARIANT 85 85 G -> A (in MTDPS9; dbSNP:rs267607097).
{ECO:0000269|PubMed:19526370}.
/FTId=VAR_065157.
VARIANT 170 170 P -> R (in MTDPS9; dbSNP:rs267607099).
{ECO:0000269|PubMed:20693550}.
/FTId=VAR_065121.
CONFLICT 19 19 S -> N (in Ref. 4; CAA92426).
{ECO:0000305}.
CONFLICT 34 34 P -> Q (in Ref. 4; CAA92426).
{ECO:0000305}.
CONFLICT 39 39 R -> Q (in Ref. 4; CAA92426).
{ECO:0000305}.
CONFLICT 87 87 T -> L (in Ref. 3; AAD17940).
{ECO:0000305}.
HELIX 43 50 {ECO:0000244|PDB:6G4Q}.
STRAND 57 62 {ECO:0000244|PDB:6G4Q}.
HELIX 66 78 {ECO:0000244|PDB:6G4Q}.
STRAND 81 86 {ECO:0000244|PDB:6G4Q}.
STRAND 98 103 {ECO:0000244|PDB:6G4Q}.
HELIX 104 111 {ECO:0000244|PDB:6G4Q}.
STRAND 115 118 {ECO:0000244|PDB:6G4Q}.
HELIX 122 134 {ECO:0000244|PDB:6G4Q}.
STRAND 138 142 {ECO:0000244|PDB:6G4Q}.
HELIX 149 159 {ECO:0000244|PDB:6G4Q}.
STRAND 166 168 {ECO:0000244|PDB:6G4Q}.
STRAND 174 177 {ECO:0000244|PDB:6G4Q}.
TURN 178 180 {ECO:0000244|PDB:6G4Q}.
STRAND 181 185 {ECO:0000244|PDB:6G4Q}.
HELIX 188 190 {ECO:0000244|PDB:6G4Q}.
STRAND 193 201 {ECO:0000244|PDB:6G4Q}.
HELIX 204 215 {ECO:0000244|PDB:6G4Q}.
STRAND 220 225 {ECO:0000244|PDB:6G4Q}.
HELIX 236 244 {ECO:0000244|PDB:6G4Q}.
STRAND 251 261 {ECO:0000244|PDB:6G4Q}.
HELIX 262 273 {ECO:0000244|PDB:6G4Q}.
STRAND 282 287 {ECO:0000244|PDB:6G4Q}.
HELIX 311 320 {ECO:0000244|PDB:6G4Q}.
HELIX 332 341 {ECO:0000244|PDB:6G4Q}.
TURN 342 344 {ECO:0000244|PDB:6G4Q}.
SEQUENCE 346 AA; 36250 MW; 76EF06F323CD5188 CRC64;
MTATLAAAAD IATMVSGSSG LAAARLLSRS FLLPQNGIRH CSYTASRQHL YVDKNTKIIC
QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGQTHLGLPV FNTVKEAKEQ TGATASVIYV
PPPFAAAAIN EAIEAEIPLV VCITEGIPQQ DMVRVKHKLL RQEKTRLIGP NCPGVINPGE
CKIGIMPGHI HKKGRIGIVS RSGTLTYEAV HQTTQVGLGQ SLCVGIGGDP FNGTDFIDCL
EIFLNDSATE GIILIGEIGG NAEENAAEFL KQHNSGPNSK PVVSFIAGLT APPGRRMGHA
GAIIAGGKGG AKEKISALQS AGVVVSMSPA QLGTTIYKEF EKRKML


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CSB-EL022919RA Rat Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial(SUCLG1) ELISA kit SpeciesRat 96T
CSB-EL022919PI Pig Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial(SUCLG1) ELISA kit SpeciesPig 96T
CSB-EL022919BO Bovine Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial(SUCLG1) ELISA kit 96T


 

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