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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_RAT                Reviewed;         346 AA.
P13086; Q6P7S4;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 2.
10-OCT-2018, entry version 156.
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};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-346.
TISSUE=Liver;
PubMed=3422742; DOI=10.1073/pnas.85.5.1432;
Henning W.D., Upton C., McFadden G., Majumdar R., Bridger W.A.;
"Cloning and sequencing of the cytoplasmic precursor to the alpha
subunit of rat liver mitochondrial succinyl-CoA synthetase.";
Proc. Natl. Acad. Sci. U.S.A. 85:1432-1436(1988).
-!- 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}.
-!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha
subunit family. {ECO:0000255|HAMAP-Rule:MF_03222}.
-!- SEQUENCE CAUTION:
Sequence=AAA41233.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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EMBL; BC061537; AAH61537.2; -; mRNA.
EMBL; J03621; AAA41233.1; ALT_SEQ; mRNA.
PIR; A28962; SYRTSA.
RefSeq; NP_446204.2; NM_053752.2.
UniGene; Rn.3766; -.
ProteinModelPortal; P13086; -.
SMR; P13086; -.
BioGrid; 250390; 2.
CORUM; P13086; -.
IntAct; P13086; 1.
STRING; 10116.ENSRNOP00000007624; -.
iPTMnet; P13086; -.
PhosphoSitePlus; P13086; -.
SwissPalm; P13086; -.
PaxDb; P13086; -.
PRIDE; P13086; -.
GeneID; 114597; -.
KEGG; rno:114597; -.
UCSC; RGD:619821; rat.
CTD; 8802; -.
RGD; 619821; Suclg1.
eggNOG; KOG1255; Eukaryota.
eggNOG; COG0074; LUCA.
HOGENOM; HOG000239685; -.
HOVERGEN; HBG000957; -.
InParanoid; P13086; -.
KO; K01899; -.
OrthoDB; EOG091G0D9C; -.
PhylomeDB; P13086; -.
TreeFam; TF300666; -.
UniPathway; UPA00223; UER00999.
PRO; PR:P13086; -.
Proteomes; UP000002494; Unplaced.
Genevisible; P13086; RN.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0045244; C:succinate-CoA ligase complex (GDP-forming); IDA:RGD.
GO; GO:0048037; F:cofactor binding; IEA:InterPro.
GO; GO:0019003; F:GDP binding; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD.
GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IDA:RGD.
GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IDA:RGD.
GO; GO:0006105; P:succinate metabolic process; IDA:RGD.
GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:RGD.
GO; GO:0006099; P:tricarboxylic acid cycle; IDA:RGD.
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.
2: Evidence at transcript level;
Acetylation; Complete proteome; Ligase; Mitochondrion;
Nucleotide-binding; Reference proteome; Transit peptide;
Tricarboxylic acid cycle.
TRANSIT 1 34 Mitochondrion. {ECO:0000255|HAMAP-
Rule:MF_03222}.
CHAIN 35 346 Succinate--CoA ligase [ADP/GDP-forming]
subunit alpha, mitochondrial.
{ECO:0000255|HAMAP-Rule:MF_03222}.
/FTId=PRO_0000033343.
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,
ECO:0000269|PubMed:3422742}.
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:0000250|UniProtKB:P53597}.
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 94 94 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}.
CONFLICT 153 153 V -> L (in Ref. 2; AAA41233).
{ECO:0000305}.
SEQUENCE 346 AA; 36148 MW; 2DDFC746C11B5B0C CRC64;
MTAAVVAAAA TATMVSGSSG LAAARLLSRT FLLQQNGIRH GSYTASRKNI YIDKNTKVIC
QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGKKHLGLPV FNTVKEAKEK TGATASVIYV
PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ DMVRVKHKLT RQGKTRLIGP NCPGIINPGE
CKIGIMPGHI HKKGRIGIVS RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTNFIDCL
DVFLKDPATE GIVLIGEIGG HAEENAAEFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA
GAIIAGGKGG AKEKISALQS AGVIVSMSPA QLGTCMYKEF EKRKML


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