(data stored in SCRATCH3701 zone)

SWISSPROT: SUCC_RICTY

ID   SUCC_RICTY              Reviewed;         386 AA.
AC   Q68WU5;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 91.
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=RT0420;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03897.1; -; Genomic_DNA.
DR   RefSeq; WP_011190881.1; NC_006142.1.
DR   SMR; Q68WU5; -.
DR   STRING; 257363.RT0420; -.
DR   PRIDE; Q68WU5; -.
DR   EnsemblBacteria; AAU03897; AAU03897; RT0420.
DR   KEGG; rty:RT0420; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; ITACDEV; -.
DR   OrthoDB; 316012at2; -.
DR   BioCyc; RTYP257363:G1G0L-427-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000000604; Chromosome.
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; Q68WU5.
DR   SWISS-2DPAGE; Q68WU5.
KW   ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..386
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT                   /id="PRO_0000102852"
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   386 AA;  41904 MW;  8FDEB965DDCC45EF CRC64;
     MNIHEYQAKE ILRKYGVPTS TGLVVTKTEK INEAIDKLNT KVYVVKAQIH AGGRGKAGGV
     KVVKSKEEAK KVAHDMFGIN LVTHQTGPQG QKVNHLYIES GCDILKEYYF SIVFDRSASC
     ITFIASTEGG VDIEAVAEKM PEKIIKFAVD PATGLQDFHM RGIAYGLGFK DSQAKQMKEI
     VKSVYNAFIE TDATQIEINP LIINSYKNLL ALDAKITFDD NGLFKHPNIT AMRDHDEEDP
     LETRAANAGL SYVKMDGNIG CMVNGAGLAM ATMDIIKLYG ASPANFLDVG GGADRERVKE
     ALKIILSDKE VKGILVNIFG GIMRCDIIAE GIIAAARDIG ITVPLVVRLA GTNVEKGKEI
     LSNSNLKIIP AHDLADAANK IVEAIR
//

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