ID E0VG44_PEDHC Unreviewed; 329 AA.
AC E0VG44;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=8236743 {ECO:0000313|EnsemblMetazoa:PHUM173270-PA};
GN ORFNames=Phum_PHUM173270 {ECO:0000313|EMBL:EEB12350.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB12350.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB12350.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB12350.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB12350.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM173270-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM173270-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) 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 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; AAZO01002010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235131; EEB12350.1; -; Genomic_DNA.
DR RefSeq; XP_002425088.1; XM_002425043.1.
DR AlphaFoldDB; E0VG44; -.
DR STRING; 121224.E0VG44; -.
DR EnsemblMetazoa; PHUM173270-RA; PHUM173270-PA; PHUM173270.
DR GeneID; 8236743; -.
DR KEGG; phu:Phum_PHUM173270; -.
DR CTD; 8236743; -.
DR VEuPathDB; VectorBase:PHUM173270; -.
DR eggNOG; KOG1255; Eukaryota.
DR HOGENOM; CLU_052104_1_0_1; -.
DR InParanoid; E0VG44; -.
DR OMA; VIICITE; -.
DR OrthoDB; 474at2759; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000009046; Unassembled WGS sequence.
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 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:UP000009046};
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 282
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"
FT BINDING 190
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
SQ SEQUENCE 329 AA; 34713 MW; 34162671AB7DABC2 CRC64;
MAASVRALLR NSACQTLKLQ NVRTNYNATR PNLKINKDTK VICQGFTGKQ GTFHSVQALE
YGTQIVGGVS PGKGGKTHLE KPVFNSVKEA MQATGATASV IYVPPPGAAK AILESIEAEM
PLIVCITEGI PQSDMVKVKH QLLRQNKSRL IGPNCPGIIA SDECKIGIMP GHIHKKGCVG
IVSRSGTLTY EAVHQTTQVG LGQTLCVGIG GDPFNGTDFI DCLECFIKDP DTKGIILIGE
IGGVAEEQAA EYLTKHNYGI KAKPVVSFIA GLSAPPGRRM GHAGAIISGG KGGAQDKIKA
LESAGVIVTK SPAKMGSELF KEMKRLELV
//
