ID B8GKV3_METPE Unreviewed; 288 AA.
AC B8GKV3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha {ECO:0000256|HAMAP-Rule:MF_01988};
DE EC=6.2.1.5 {ECO:0000256|HAMAP-Rule:MF_01988};
DE AltName: Full=Succinyl-CoA synthetase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01988};
DE Short=SCS-alpha {ECO:0000256|HAMAP-Rule:MF_01988};
GN Name=sucD {ECO:0000256|HAMAP-Rule:MF_01988};
GN OrderedLocusNames=Mpal_1945 {ECO:0000313|EMBL:ACL17249.1};
OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX NCBI_TaxID=521011 {ECO:0000313|EMBL:ACL17249.1, ECO:0000313|Proteomes:UP000002457};
RN [1] {ECO:0000313|EMBL:ACL17249.1, ECO:0000313|Proteomes:UP000002457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c
RC {ECO:0000313|Proteomes:UP000002457};
RX PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA Yavitt J.B., Zinder S.H.;
RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL Genome Announc. 3:e01280-15(2015).
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 nucleotide specificity is provided by the beta subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000699}.
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_01988, ECO:0000256|RuleBase:RU000699};
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; Evidence={ECO:0000256|HAMAP-Rule:MF_01988};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC from succinyl-CoA (ligase route): step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01988, ECO:0000256|RuleBase:RU000699}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000699}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000256|HAMAP-Rule:MF_01988,
CC ECO:0000256|RuleBase:RU000677}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01988}.
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DR EMBL; CP001338; ACL17249.1; -; Genomic_DNA.
DR RefSeq; WP_012618568.1; NC_011832.1.
DR AlphaFoldDB; B8GKV3; -.
DR STRING; 521011.Mpal_1945; -.
DR GeneID; 7270749; -.
DR KEGG; mpl:Mpal_1945; -.
DR eggNOG; arCOG01339; Archaea.
DR HOGENOM; CLU_052104_0_0_2; -.
DR OrthoDB; 55711at2157; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000002457; Chromosome.
DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
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:RHEA.
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 3: Inferred from homology;
KW Ligase {ECO:0000256|HAMAP-Rule:MF_01988, ECO:0000256|RuleBase:RU000677};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01988}; Reference proteome {ECO:0000313|Proteomes:UP000002457};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_01988}.
FT DOMAIN 4..104
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 247
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988,
FT ECO:0000256|PIRSR:PIRSR001553-1"
FT BINDING 16..19
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT BINDING 100..102
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT BINDING 163
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
SQ SEQUENCE 288 AA; 29669 MW; 2B1693761DAE76C5 CRC64;
MIYGDKSLGV IVQGATGKQG AFHINLMNEY ARSVGGRGVV AGVTPGRGGQ EVHGVPVYNS
VHEALAEHDA TASVLFVPGK AAGDSIMEAA SAGLELVVAI TEHIPVHDTM KAVAYAKLHD
CAVIGPNCPG LLSPGEVKLG IMPAHLFTRG HVGVISRSGT LTYEIVDELT RAGIGQSTVV
GIGGDPVIGQ TFVDLLDRFE EDPETRAVVL VGEVGGALEQ EGAASTDLPI VAYIAGVSAP
PDKRMGHAGA IVEGGEGDAG SKIRHLQNQG VTVAQRPSEI PCLIRNLL
//
