(data stored in ACNUC7421 zone)

SWISSPROT: SUCC_DESOH

ID   SUCC_DESOH              Reviewed;         388 AA.
AC   A8ZRW7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   11-DEC-2019, entry version 78.
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=Dole_0074;
OS   Desulfococcus oleovorans (strain DSM 6200 / Hxd3).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulfococcus.
OX   NCBI_TaxID=96561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / Hxd3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-2007) 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; CP000859; ABW65884.1; -; Genomic_DNA.
DR   RefSeq; WP_012173503.1; NC_009943.1.
DR   SMR; A8ZRW7; -.
DR   STRING; 96561.Dole_0074; -.
DR   EnsemblBacteria; ABW65884; ABW65884; Dole_0074.
DR   KEGG; dol:Dole_0074; -.
DR   eggNOG; ENOG4105CMV; Bacteria.
DR   eggNOG; COG0045; LUCA.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; ITACDEV; -.
DR   OrthoDB; 316012at2; -.
DR   BioCyc; DOLE96561:G1GAC-75-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   Proteomes; UP000008561; 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; A8ZRW7.
DR   SWISS-2DPAGE; A8ZRW7.
KW   ATP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..388
FT                   /note="Succinate--CoA ligase [ADP-forming] subunit beta"
FT                   /id="PRO_1000129181"
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   388 AA;  40793 MW;  D601C93C944E75F7 CRC64;
     MKIHEFQTKE LFRTYGIPTP EGRMVNTAEA AGEAAGELGG FPVVVKAQIH AGGRGKGGGV
     KLAKSADEAK SLAGAMLGSR LVTPQTGPEG TLVQKVLVEQ GVSIAKELYL SVVADRETAG
     IVIMASEAGG MDIEAVAETT PEKILKVFVN PLAGLSAFHC RQAAYGLNLP AEAIKPFTQV
     VSGLFKLFVD YDASLVEINP LILTTDKAVM ALDAKINFDD SALFRHKDIL ALRDTDEEDP
     LEVEASRFNL NYINMDGNVG NMVNGAGLAM ATMDIIKLAG AEPANFLDVG GGANAEMVEN
     GFRIILSDPK VKCILVNIFG GILRCDVLAS GIVQAARNTA IHVPLVVRME GTNVDEGKRI
     LAESGLDLHS AASLKDAAAR VAQVVAAA
//

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