SUCA_BOVIN
ID SUCA_BOVIN Reviewed; 346 AA.
AC Q58DR8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 97.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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}.
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DR EMBL; BT021529; AAX46376.1; -; mRNA.
DR RefSeq; NP_001030254.1; NM_001035082.1.
DR AlphaFoldDB; Q58DR8; -.
DR SMR; Q58DR8; -.
DR IntAct; Q58DR8; 1.
DR STRING; 9913.ENSBTAP00000007982; -.
DR PaxDb; Q58DR8; -.
DR PeptideAtlas; Q58DR8; -.
DR PRIDE; Q58DR8; -.
DR GeneID; 509983; -.
DR KEGG; bta:509983; -.
DR CTD; 8802; -.
DR eggNOG; KOG1255; Eukaryota.
DR InParanoid; Q58DR8; -.
DR OrthoDB; 1247548at2759; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT CHAIN 28..346
FT /note="Succinate--CoA ligase [ADP/GDP-forming] subunit
FT alpha, mitochondrial"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT /id="PRO_0000270820"
FT ACT_SITE 299
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
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 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 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"
SQ SEQUENCE 346 AA; 36167 MW; 4DCBBC980F23AA60 CRC64;
MTAALAAARA AATMASGSSG LAAARLLSRA FLLQQNGIRH CSYTTSRKHL YVDRNTKIIC
QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGKTHLGLPV FNTVKEAKEQ TGATASVIYV
PPPFAVAAID EAIEAEVSLV VCITEGIPQQ DMVRVKHKLL RQGKTRLVGP NCPGVINPGE
CKIGIMPGHI HKKGRVGIVS RSGTLTYEAV HQTTQVGLGQ SLCVGIGGDP FNGTDFTDCL
EIFLNDPATE GIILIGEIGG NAEENAAEFL KQHNSGPKAK PVVSFIAGLT APPGRRMGHA
GAIIAGGKGG AKEKIAALQS AGVVVSMSPA QLGTTMYKEF EKRKML
