SUCA_RAT
ID SUCA_RAT Reviewed; 346 AA.
AC P13086; Q6P7S4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03222};
DE EC=6.2.1.4 {ECO:0000255|HAMAP-Rule:MF_03222};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_03222};
DE AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE Short=SCS-alpha {ECO:0000255|HAMAP-Rule:MF_03222};
DE Flags: Precursor;
GN Name=Suclg1 {ECO:0000255|HAMAP-Rule:MF_03222};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-346.
RC TISSUE=Liver;
RX PubMed=3422742; DOI=10.1073/pnas.85.5.1432;
RA Henning W.D., Upton C., McFadden G., Majumdar R., Bridger W.A.;
RT "Cloning and sequencing of the cytoplasmic precursor to the alpha subunit
RT of rat liver mitochondrial succinyl-CoA synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1432-1436(1988).
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle
CC (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of
CC either ATP or GTP and thus represents the only step of substrate-level
CC phosphorylation in the TCA. The alpha subunit of the enzyme binds the
CC substrates coenzyme A and phosphate, while succinate binding and
CC specificity for either ATP or GTP is provided by different beta
CC subunits. {ECO:0000255|HAMAP-Rule:MF_03222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03222};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03222}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Different beta
CC subunits determine nucleotide specificity. Together with the ATP-
CC specific beta subunit SUCLA2, forms an ADP-forming succinyl-CoA
CC synthetase (A-SCS). Together with the GTP-specific beta subunit SUCLG2
CC forms a GDP-forming succinyl-CoA synthetase (G-SCS).
CC {ECO:0000255|HAMAP-Rule:MF_03222}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_03222}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA41233.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; BC061537; AAH61537.2; -; mRNA.
DR EMBL; J03621; AAA41233.1; ALT_SEQ; mRNA.
DR PIR; A28962; SYRTSA.
DR RefSeq; NP_446204.2; NM_053752.2.
DR AlphaFoldDB; P13086; -.
DR SMR; P13086; -.
DR BioGRID; 250390; 6.
DR CORUM; P13086; -.
DR IntAct; P13086; 8.
DR MINT; P13086; -.
DR STRING; 10116.ENSRNOP00000007624; -.
DR iPTMnet; P13086; -.
DR PhosphoSitePlus; P13086; -.
DR SwissPalm; P13086; -.
DR jPOST; P13086; -.
DR PaxDb; P13086; -.
DR PRIDE; P13086; -.
DR GeneID; 114597; -.
DR KEGG; rno:114597; -.
DR UCSC; RGD:619821; rat.
DR CTD; 8802; -.
DR RGD; 619821; Suclg1.
DR eggNOG; KOG1255; Eukaryota.
DR HOGENOM; CLU_052104_1_0_1; -.
DR InParanoid; P13086; -.
DR OrthoDB; 1247548at2759; -.
DR PhylomeDB; P13086; -.
DR TreeFam; TF300666; -.
DR Reactome; R-RNO-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00999.
DR PRO; PR:P13086; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P13086; RN.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0009361; C:succinate-CoA ligase complex (ADP-forming); IBA:GO_Central.
DR GO; GO:0045244; C:succinate-CoA ligase complex (GDP-forming); IDA:RGD.
DR GO; GO:0019003; F:GDP binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IDA:RGD.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IDA:RGD.
DR GO; GO:0006105; P:succinate metabolic process; IDA:RGD.
DR GO; GO:0006104; P:succinyl-CoA metabolic process; IDA:RGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:RGD.
DR Gene3D; 3.40.50.261; -; 1.
DR HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005810; CoA_lig_alpha.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001553; SucCS_alpha; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF52210; SSF52210; 1.
DR TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT CHAIN 35..346
FT /note="Succinate--CoA ligase [ADP/GDP-forming] subunit
FT alpha, mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT /id="PRO_0000033343"
FT ACT_SITE 299
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222,
FT ECO:0000269|PubMed:3422742"
FT BINDING 64..67
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 90
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 143..145
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 207
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P53597"
FT MOD_RES 57
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT MOD_RES 57
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT MOD_RES 66
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT MOD_RES 66
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT MOD_RES 94
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT MOD_RES 338
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9WUM5"
FT CONFLICT 153
FT /note="V -> L (in Ref. 2; AAA41233)"
FT /evidence="ECO:0000305"
SQ 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
