(data stored in SCRATCH zone)

SWISSPROT: D1CE54_THET1

ID   D1CE54_THET1            Unreviewed;       290 AA.
AC   D1CE54;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAY-2019, entry version 70.
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=Tter_0288 {ECO:0000313|EMBL:ACZ41210.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41210.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41210.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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:
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   -!- 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; CP001825; ACZ41210.1; -; Genomic_DNA.
DR   RefSeq; WP_012874245.1; NC_013525.1.
DR   STRING; 525904.Tter_0288; -.
DR   EnsemblBacteria; ACZ41210; ACZ41210; Tter_0288.
DR   KEGG; ttr:Tter_0288; -.
DR   eggNOG; ENOG4105CH8; Bacteria.
DR   eggNOG; COG0074; LUCA.
DR   HOGENOM; HOG000239685; -.
DR   KO; K01902; -.
DR   OMA; IIFVPPA; -.
DR   OrthoDB; 1081709at2; -.
DR   BioCyc; TTER525904:G1GGS-291-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000000323; Chromosome 1.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
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; 3.40.50.261; -; 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; IPR036291; NAD(P)-bd_dom_sf.
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; D1CE54.
DR   SWISS-2DPAGE; D1CE54.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000323};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000677};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000699};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01988,
KW   ECO:0000256|RuleBase:RU000699}.
FT   DOMAIN        4    100       CoA_binding. {ECO:0000259|SMART:SM00881}.
FT   REGION       17     20       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01988}.
FT   REGION       96     98       Coenzyme A binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01988}.
FT   ACT_SITE    246    246       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01988,
FT                                ECO:0000256|PIRSR:PIRSR001553-1}.
FT   BINDING     159    159       Substrate; shared with subunit beta.
FT                                {ECO:0000256|HAMAP-Rule:MF_01988}.
SQ   SEQUENCE   290 AA;  29951 MW;  14A95FBB977C6A6A CRC64;
     MSILVDKNTR LLVQGITGRE GSFHTQQMVE YGTNVVAGVT PGAAGREVCG VPVYNTVREA
     VEATGANTSI VYVPAPFAPD AVYEAASAGI SLIVCITEHI PAVDEVKMYH YVREKGSRLI
     GPNCPGLTTP GEAKVGIIPG NIHKRGPVGI VSRSGTLTYE AVAALTAADI GQSTVVGIGG
     DPIVGTSFRE VLEMFEDDPE THAVVLIGEI GGNAEEEAAE YIRQMTKPVV AFIAGRTAPP
     GRRMGHAGAI ISGGSGTAES KIRALEGANA HIAETPSQIA ELVEVALAGA
//

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