(data stored in SCRATCH zone)

SWISSPROT: C4KKW3_SULIK

ID   C4KKW3_SULIK            Unreviewed;       260 AA.
AC   C4KKW3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   30-AUG-2017, entry version 53.
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=M164_0294 {ECO:0000313|EMBL:ACR40928.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40928.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40928.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid
CC       cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC       synthesis of either ATP or GTP and thus represents the only step
CC       of substrate-level phosphorylation in the TCA. The alpha subunit
CC       of the enzyme binds the substrates coenzyme A and phosphate, while
CC       succinate binding and nucleotide specificity is provided by the
CC       beta subunit. {ECO:0000256|HAMAP-Rule:MF_01988,
CC       ECO:0000256|RuleBase:RU000699}.
CC   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA. {ECO:0000256|HAMAP-Rule:MF_01988,
CC       ECO:0000256|RuleBase:RU000699}.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000256|HAMAP-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
CC       subunit family. {ECO:0000256|HAMAP-Rule:MF_01988,
CC       ECO:0000256|RuleBase:RU000677}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01988}.
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DR   EMBL; CP001402; ACR40928.1; -; Genomic_DNA.
DR   RefSeq; WP_012735445.1; NC_012726.1.
DR   ProteinModelPortal; C4KKW3; -.
DR   EnsemblBacteria; ACR40928; ACR40928; M164_0294.
DR   KEGG; sid:M164_0294; -.
DR   HOGENOM; HOG000239685; -.
DR   KO; K01902; -.
DR   OMA; IIFVPPA; -.
DR   OrthoDB; POG093Z0657; -.
DR   BioCyc; SISL426118:GI01-296-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.261; -; 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; IPR005811; CoA_ligase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KKW3.
DR   SWISS-2DPAGE; C4KKW3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000699, ECO:0000313|EMBL:ACR40928.1};
KW   Lyase {ECO:0000313|EMBL:ACR40928.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000699};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000699}.
FT   DOMAIN        1     73       CoA_binding. {ECO:0000259|SMART:SM00881}.
FT   REGION       69     71       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01988}.
FT   ACT_SITE    221    221       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01988,
FT                                ECO:0000256|PIRSR:PIRSR001553-1}.
FT   BINDING      16     16       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01988}.
FT   BINDING     132    132       Substrate; shared with subunit beta.
FT                                {ECO:0000256|HAMAP-Rule:MF_01988}.
SQ   SEQUENCE   260 AA;  27790 MW;  C0F31226C1D9CF2F CRC64;
     MLKYGTKIVA GVTPGKGGTQ VNNVPVYDTV KDAMKEHEAD TSIIFVPARY AVDAIYEAVD
     AGIKLIVTIT EHIPVLDMAR AIKYARARGA RIIGPNCPGI IAPEESLVGI LPARAFKKGK
     IGIVSRSGTL TYEVSELLKN SGMGQSTVIG IGGDPIIGTS TLEVAKMFDQ DPETEKIVVI
     GEIGGTMEER LAEAYKRGEI KKPIIAYIAG MTAPREKRMG HAGAVVYMGM GTFESKIRAF
     KEAGIPIANT PYDIPKLLLS
//

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