SUCA_COLLI
ID SUCA_COLLI Reviewed; 306 AA.
AC Q9YGD2;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 94.
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: Fragment;
GN Name=SUCLG1 {ECO:0000255|HAMAP-Rule:MF_03222};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver, and Skeletal muscle;
RX PubMed=9765291; DOI=10.1074/jbc.273.42.27580;
RA Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.;
RT "Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA
RT synthetases in multicellular eucaryotes.";
RL J. Biol. Chem. 273:27580-27586(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9765290; DOI=10.1074/jbc.273.42.27573;
RA Johnson J.D., Muhonen W.W., Lambeth D.O.;
RT "Characterization of the ATP- and GTP-specific succinyl-CoA synthetases in
RT pigeon. The enzymes incorporate the same alpha-subunit.";
RL J. Biol. Chem. 273:27573-27579(1998).
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 ECO:0000269|PubMed:9765290}.
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, ECO:0000269|PubMed:9765290};
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, ECO:0000269|PubMed:9765290};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.1 mM for succinate (for A-SCS) {ECO:0000269|PubMed:9765290};
CC KM=0.032 mM for CoA (for A-SCS) {ECO:0000269|PubMed:9765290};
CC KM=0.041 mM for succinyl-CoA (for A-SCS)
CC {ECO:0000269|PubMed:9765290};
CC KM=0.72 mM for phosphate (for A-SCS) {ECO:0000269|PubMed:9765290};
CC KM=4.9 mM for succinate (for G-SCS) {ECO:0000269|PubMed:9765290};
CC KM=0.036 mM for CoA (for G-SCS) {ECO:0000269|PubMed:9765290};
CC KM=0.086 mM for succinyl-CoA (for G-SCS)
CC {ECO:0000269|PubMed:9765290};
CC KM=2.26 mM for phosphate (for G-SCS) {ECO:0000269|PubMed:9765290};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_03222, ECO:0000305|PubMed:9765290}.
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, ECO:0000269|PubMed:9765290}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222,
CC ECO:0000305|PubMed:9765290}.
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; AF035393; AAD02018.1; -; mRNA.
DR EMBL; AF035394; AAD02019.1; -; mRNA.
DR AlphaFoldDB; Q9YGD2; -.
DR SMR; Q9YGD2; -.
DR STRING; 8932.XP_005510017.1; -.
DR eggNOG; KOG1255; Eukaryota.
DR SABIO-RK; Q9YGD2; -.
DR UniPathway; UPA00223; UER00999.
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-EC.
DR GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 1: Evidence at protein level;
KW Ligase; Mitochondrion; Nucleotide-binding; Tricarboxylic acid cycle.
FT CHAIN <1..306
FT /note="Succinate--CoA ligase [ADP/GDP-forming] subunit
FT alpha, mitochondrial"
FT /id="PRO_0000413700"
FT ACT_SITE 259
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 24..27
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 50
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 103..105
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT BINDING 167
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03222"
FT NON_TER 1
SQ SEQUENCE 306 AA; 32052 MW; 856BA782E49FBAE6 CRC64;
CSYSASRKNL YISKNTKVIC QGFTGKQGTF HSQQALDYGT NLVGGISPGK GGKTHLGLPV
FNSVKEAKEQ TGASATVIYV PPPFAAAAIN EAIDAEMPLV VCITEGIPQQ DMVRVKHRLV
RQDKTRLVGP NCPGVINPGE CKIGIMPGHI HKKGRIGIVS RSGTLTYEAV HQTSQVGLGQ
SLCIGIGGDP FNGTNFIDCL DVFLKDPHTE GIILIGEIGG NAEEDAAAFL KENNSGPNAK
PVVSFIAGLT APPGRRMGHA GAIIAGGKGG AKEKIAALQN AGVVVSMSPA QLGSTIYKEF
EKRKLL
