ID C1BUU8_LEPSM Unreviewed; 327 AA.
AC C1BUU8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
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=SUCA {ECO:0000313|EMBL:ACO12801.1};
GN Synonyms=Scsalpha {ECO:0000313|EMBL:CDW38387.1};
GN ORFNames=LSAA_6241 {ECO:0000313|EMBL:CAF2867906.1};
OS Lepeophtheirus salmonis (Salmon louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Hexanauplia; Copepoda; Siphonostomatoida; Caligidae; Lepeophtheirus.
OX NCBI_TaxID=72036 {ECO:0000313|EMBL:ACO12801.1};
RN [1] {ECO:0000313|EMBL:ACO12801.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Pacific form {ECO:0000313|EMBL:ACO12801.1};
RC TISSUE=Whole {ECO:0000313|EMBL:ACO12801.1};
RA Yasuike M., von Schalburg K., Cooper G., Leong J., Jones S.R.M., Koop B.F.;
RT "Lepeophtheirus salmonis ESTs and full-length cDNAs.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADD38307.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Atlantic form {ECO:0000313|EMBL:ADD38307.1};
RC TISSUE=Mixed tissue {ECO:0000313|EMBL:ADD38307.1};
RA Yasuike M., von Schalburg K., Cooper G., Leong J., Nilsen F., Jones S.R.M.,
RA Koop B.F.;
RT "Atlantic Lepeophtheirus salmonis ESTs and full-length cDNAs.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:CDW38387.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole organism {ECO:0000313|EMBL:CDW38387.1};
RA Chronopoulou M.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CAF2867906.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IoA-00 {ECO:0000313|EMBL:CAF2867906.1};
RA Bekaert M.;
RL Submitted (FEB-2021) to the EMBL/GenBank/DDBJ databases.
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 an ATP-
CC specific beta subunit, forms an ADP-forming succinyl-CoA synthetase (A-
CC SCS). Together with a GTP-specific beta subunit forms a GDP-forming
CC succinyl-CoA synthetase (G-SCS). {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}.
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DR EMBL; BT078377; ACO12801.1; -; mRNA.
DR EMBL; BT121377; ADD38307.1; -; mRNA.
DR EMBL; HG994581; CAF2867906.1; -; Genomic_DNA.
DR EMBL; HACA01021026; CDW38387.1; -; Transcribed_RNA.
DR AlphaFoldDB; C1BUU8; -.
DR EnsemblMetazoa; XM_040707483.1; XP_040563417.1; LOC121113647.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000675881; Chromosome 2.
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; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005810; CoA_lig_alpha.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005811; SUCC_ACL_C.
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; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 2: Evidence at transcript level;
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:UP000675881};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_03222}.
FT DOMAIN 32..128
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 280
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222,
FT ECO:0000256|PIRSR:PIRSR001553-1"
FT BINDING 45..48
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
FT BINDING 71
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
FT BINDING 124..126
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
FT BINDING 188
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
SQ SEQUENCE 327 AA; 33963 MW; 95EFF9EBA35DC466 CRC64;
MAASFRIFQR FSVPGSINGV RSCYSKTNMN MMLTKDSKVI CQGFTGKQGT FHSQQAIDYG
TNMVGGVSPK KAGQTHLGLP VFGSVKEAVQ KTNADATVIY VPPPGAAAAI LEAVEAEIGL
IVCITEGIPQ QDMVRVKDAL IQQSKSRLIG PNCPGIIAPN KCKIGIMPGH IHQEGCIGVV
SRSGTLTYEA VHQTTQVGLG QTLCIGIGGD PFNGTNFIDC LDIFLKDPKT KGIIMIGEIG
GAAEEKAADY LQEHNSGANQ KPVVSFIAGV TAPPGRRMGH AGAIISGGKG TAQTKIAALE
AAGVAVTSSP AKMGTTLVQL MKESGLA
//
