(data stored in SCRATCH zone)

SWISSPROT: B7ULK5_ECO27

ID   B7ULK5_ECO27            Unreviewed;       289 AA.
AC   B7ULK5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 73.
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:CAS08156.1};
GN   OrderedLocusNames=E2348C_0608 {ECO:0000313|EMBL:CAS08156.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS08156.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS08156.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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:
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}.
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DR   EMBL; FM180568; CAS08156.1; -; Genomic_DNA.
DR   RefSeq; WP_000025456.1; NC_011601.1.
DR   EnsemblBacteria; CAS08156; CAS08156; E2348C_0608.
DR   KEGG; ecg:E2348C_0608; -.
DR   HOGENOM; HOG000239685; -.
DR   KO; K01902; -.
DR   OMA; IIFVPPA; -.
DR   BioCyc; ECOL574521:E2348C_RS03230-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000008205; Chromosome.
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; B7ULK5.
DR   SWISS-2DPAGE; B7ULK5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
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   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    247    247       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01988,
FT                                ECO:0000256|PIRSR:PIRSR001553-1}.
FT   BINDING      43     43       Coenzyme A. {ECO:0000256|HAMAP-Rule:
FT                                MF_01988}.
FT   BINDING     159    159       Substrate; shared with subunit beta.
FT                                {ECO:0000256|HAMAP-Rule:MF_01988}.
SQ   SEQUENCE   289 AA;  29789 MW;  33C3863528A15835 CRC64;
     MSILIDKNTK VICQGFTGSQ GTFHSEQAIA YGTKMVGGVT PGKGGTTHLG LPVFNTVREA
     VAATGATASV IYVPAPFCKD SILEAIDAGI KLIITITEGI PTLDMLIVKV KLDEAGVRMI
     GPNCPGVITP GECKIGIQPG HIHKPGKVGI VSRSGTLTYE AVKQTTDYGF GQSTCVGIGG
     DPIPGSNFID ILEMFEKDPQ TEAIVMIGEI GGSAEEEAAA YIKEHVTKPV VGYIAGVTAP
     KGKRMGHAGA IIAGGKGTAD EKFAALEAAG VKTVRSLADI GEALKTVLQ
//

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