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Database: UniProt
Entry: A0A3Q3G415_9LABR
LinkDB: A0A3Q3G415_9LABR
Original site: A0A3Q3G415_9LABR 
ID   A0A3Q3G415_9LABR        Unreviewed;       328 AA.
AC   A0A3Q3G415;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03222};
DE            EC=6.2.1.4 {ECO:0000256|HAMAP-Rule:MF_03222};
DE            EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_03222};
DE   AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000256|HAMAP-Rule:MF_03222};
DE            Short=SCS-alpha {ECO:0000256|HAMAP-Rule:MF_03222};
GN   Name=SUCLG1 {ECO:0000256|HAMAP-Rule:MF_03222};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000027821.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000027821.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|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:0000256|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:0000256|HAMAP-
CC         Rule:MF_03222};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03222}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03222}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC       family. {ECO:0000256|HAMAP-Rule:MF_03222,
CC       ECO:0000256|RuleBase:RU000677}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_03222}.
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DR   AlphaFoldDB; A0A3Q3G415; -.
DR   STRING; 56723.ENSLBEP00000027821; -.
DR   Ensembl; ENSLBET00000029148.1; ENSLBEP00000027821.1; ENSLBEG00000021066.1.
DR   GeneTree; ENSGT00940000156351; -.
DR   InParanoid; A0A3Q3G415; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000261660; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
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   NCBIfam; TIGR01019; sucCoAalpha; 1.
DR   PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP/GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   3: Inferred from homology;
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_03222, ECO:0000256|RuleBase:RU000677};
KW   Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03222};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_03222}; Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_03222}.
FT   DOMAIN          34..130
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
FT   ACT_SITE        278
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03222,
FT                   ECO:0000256|PIRSR:PIRSR001553-1"
FT   BINDING         47..50
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
FT   BINDING         73
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
FT   BINDING         126..128
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
SQ   SEQUENCE   328 AA;  34739 MW;  7A6EEF34E82C2CF5 CRC64;
     MLACSQGRAS RYFLFSVQQC GVRHCYTASR QNLYIDKNTK VICQGFTGKQ GTFHSQQSLD
     YGSQLVGGVS PGKGGKTHLG LPVFNSVKEA KDGTGADATV IYVPPPFAAA AIIEAIDAEI
     PLVVCITEGI PQQDMVRVKH KLLRQGTTRL IGPNCPGVIN PGECKIGIMP GHIHKKGRIG
     EVSCLVCWSE HSTYNERLLY LLLGIGGDPF NGTNFIDCLE VFLRDPKTEG IILIGEIGGN
     AEENAAEYLK QHNSGANAKP VVSFIAGLTA PPGRRMGHAG AIIAGGKGGA KEKIAALQSA
     GVVVSMSPAQ LGSTIFKVSP FVPARKMI
//
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