(data stored in ACNUC7421 zone)

SWISSPROT: SUCC_LEGPC

ID   SUCC_LEGPC              Reviewed;         387 AA.
AC   A5IH21;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 77.
DE   RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE            EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558};
DE   AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE            Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558};
GN   Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558}; OrderedLocusNames=LPC_2768;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) 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
CC       either ATP or GTP and thus represents the only step of substrate-level
CC       phosphorylation in the TCA. The beta subunit provides nucleotide
CC       specificity of the enzyme and binds the substrate succinate, while the
CC       binding sites for coenzyme A and phosphate are found in the alpha
CC       subunit. {ECO:0000255|HAMAP-Rule:MF_00558}.
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:0000255|HAMAP-
CC         Rule:MF_00558};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00558};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate
CC       from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00558}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00558}.
DR   EMBL; CP000675; ABQ56671.1; -; Genomic_DNA.
DR   RefSeq; WP_011214776.1; NC_009494.2.
DR   SMR; A5IH21; -.
DR   EnsemblBacteria; ABQ56671; ABQ56671; LPC_2768.
DR   KEGG; lpc:LPC_2768; -.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; ITACDEV; -.
DR   BioCyc; LPNE400673:LPC_RS03125-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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; 3.30.1490.20; -; 1.
DR   Gene3D; 3.40.50.261; -; 1.
DR   HAMAP; MF_00558; Succ_CoA_beta; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11815; PTHR11815; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5IH21.
DR   SWISS-2DPAGE; A5IH21.
KW   ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..387
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT                   /id="PRO_1000082113"
FT   DOMAIN          9..244
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   NP_BIND         53..55
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   REGION          321..323
FT                   /note="Substrate binding; shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   METAL           199
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   METAL           213
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         46
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         99
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         102
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         107
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
FT   BINDING         264
FT                   /note="Substrate; shared with subunit alpha"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00558"
SQ   SEQUENCE   387 AA;  41723 MW;  F8D14AC539F08D89 CRC64;
     MNLHEYQAKQ LFASYGLPVP RGEVAYNVED ALLVASQLST SRWVVKAQVH AGGRGKAGGV
     KLVSSKDELA AVAKSMLGTR LVTYQTDARG QPVNAILVEE TCEIDKELYL GAVVDRSTRR
     VVIMASTEGG VEIEKVAHET PEKIFKVVVD PLVGVMPFQC RETAFKLGLK DDQIKQFTHL
     MMGLGKMFVD CDLSLLEINP LVITKSGQLI CLDGKINIDG NALFRQPKLK NMRDVSQEDD
     RENRASDWEL NYIPLDGTIG CMVNGAGLAM ATMDVIKLHG GEPANFLDVG GGATKERVSE
     ALKIIVSDEK VKGILVNIFG GIVRCDLIAD GILAAVKEVD VKIPVVVRLE GNNAQLGAEI
     LNKSNLNVIA ATSLTDAAKK IVAAVSE
//

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