ID A0A2A9M8M5_9APIC Unreviewed; 332 AA.
AC A0A2A9M8M5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial {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 ORFNames=BESB_019840 {ECO:0000313|EMBL:PFH32043.1};
OS Besnoitia besnoiti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Besnoitia.
OX NCBI_TaxID=94643 {ECO:0000313|EMBL:PFH32043.1, ECO:0000313|Proteomes:UP000224006};
RN [1] {ECO:0000313|EMBL:PFH32043.1, ECO:0000313|Proteomes:UP000224006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bb-Ger1 {ECO:0000313|EMBL:PFH32043.1,
RC ECO:0000313|Proteomes:UP000224006};
RA Schares G., Venepally P., Lorenzi H.A.;
RT "Genome sequencing of Besnoitia besnoiti strain Bb-Ger1.";
RL Submitted (SEP-2017) 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 ATP
CC and thus represents the only step of substrate-level phosphorylation in
CC the TCA. The alpha subunit of the enzyme binds the substrates coenzyme
CC A and phosphate, while succinate binding and nucleotide specificity is
CC provided by the beta subunit. {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 -!- 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.
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFH32043.1}.
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DR EMBL; NWUJ01000012; PFH32043.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9M8M5; -.
DR STRING; 94643.A0A2A9M8M5; -.
DR VEuPathDB; ToxoDB:BESB_019840; -.
DR OrthoDB; 474at2759; -.
DR UniPathway; UPA00223; UER00999.
DR Proteomes; UP000224006; Chromosome xi.
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: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:UP000224006};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_03222}.
FT DOMAIN 33..135
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT ACT_SITE 285
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222,
FT ECO:0000256|PIRSR:PIRSR001553-1"
FT BINDING 46..49
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
FT BINDING 72
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
FT BINDING 131..133
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
FT BINDING 195
FT /ligand="substrate"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03222"
SQ SEQUENCE 332 AA; 35216 MW; C0180CA7D6B8A2DA CRC64;
MASPLQRVVP SGGLFRRLST ELPRRWSSTA RVFVDKNTKV ICQGLTGKQG SFHTEQCLAY
GTQFVGGVNP SKKGTMWQSS DEKFSLPVFG SVKEAKEATG CDASMIFVPP PFAAKAILDC
IAEEIPLAVC ITEGIPQQDM VRVKQALLSQ NKTRLIGPNC PGIIKPGECK IGIMPGYIHQ
KGKIGVVSRS GTLTYEAVNQ TTQAGLGQST CVGIGGDPFN GTNFIDCLER FVNDPETKGI
VLIGEIGGSA EEEAAAWLKE HNKERKPVVS FIAGLTAPPG RRMGHAGAIV SGGKGTAEGK
IAALEDAGVH VVRNPASMGQ KMLEVMKEAG LH
//
