ID   Q9YD40_AERPE            Unreviewed;       292 AA.
AC   Q9YD40;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 2.
DT   27-MAR-2024, entry version 151.
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   ECO:0000313|EMBL:BAA80057.2};
GN   OrderedLocusNames=APE_1072.1 {ECO:0000313|EMBL:BAA80057.2};
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557 {ECO:0000313|EMBL:BAA80057.2, ECO:0000313|Proteomes:UP000002518};
RN   [1] {ECO:0000313|EMBL:BAA80057.2, ECO:0000313|Proteomes:UP000002518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1
RC   {ECO:0000313|Proteomes:UP000002518};
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
RN   [2] {ECO:0007829|PDB:2YV2}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RA   Niwa H., Kuramitsu S., Yokoyama S.;
RT   "Crystal Structure of Succinyl-CoA Synthetase Alpha Chain from Aeropyrum
RT   pernix K1.";
RL   Submitted (APR-2007) to the PDB data bank.
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}.
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DR   EMBL; BA000002; BAA80057.2; -; Genomic_DNA.
DR   PIR; A72707; A72707.
DR   PDB; 2YV2; X-ray; 2.20 A; A=1-292.
DR   PDBsum; 2YV2; -.
DR   AlphaFoldDB; Q9YD40; -.
DR   SMR; Q9YD40; -.
DR   STRING; 272557.APE_1072.1; -.
DR   EnsemblBacteria; BAA80057; BAA80057; APE_1072.1.
DR   KEGG; ape:APE_1072.1; -.
DR   PATRIC; fig|272557.25.peg.754; -.
DR   eggNOG; arCOG01339; Archaea.
DR   UniPathway; UPA00223; UER00999.
DR   EvolutionaryTrace; Q9YD40; -.
DR   Proteomes; UP000002518; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2YV2};
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:UP000002518};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_01988}.
FT   DOMAIN          4..101
FT                   /note="CoA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00881"
FT   ACT_SITE        249
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988,
FT                   ECO:0000256|PIRSR:PIRSR001553-1"
FT   BINDING         17..20
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT   BINDING         43
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT   BINDING         97..99
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared with subunit beta"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01988"
SQ   SEQUENCE   292 AA;  30897 MW;  C6D0BFC049CE1F75 CRC64;
     MAVLVDSETR VLVQGITGRE GSFHAKAMLE YGTKVVAGVT PGKGGSEVHG VPVYDSVKEA
     LAEHPEINTS IVFVPAPFAP DAVYEAVDAG IRLVVVITEG IPVHDTMRFV NYARQKGATI
     IGPNCPGAIT PGQAKVGIMP GHIFKEGGVA VVSRSGTLTY EISYMLTRQG IGQSTVIGIG
     GDPIVGLSFT EALKLFQEDP QTEALVLIGE IGGDMEERAA EMIKKGEFTK PVIAYIAGRT
     APPEKRMGHA GAIIMMGTGT YEGKVKALRE AGVEVAETPF EVPELVRKAL RR
//