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Database: UniProt
Entry: Q6ARL2
LinkDB: Q6ARL2
Original site: Q6ARL2 
ID   SUCC_DESPS              Reviewed;         386 AA.
AC   Q6ARL2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   26-NOV-2014, entry version 78.
DE   RecName: Full=Succinyl-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=DP0284;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfobulbaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSv54 / DSM 12343;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M.,
RA   Bauer M., Zibat A., Lombardot T., Becker I., Amann J., Gellner K.,
RA   Teeling H., Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R.,
RA   Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium
RT   from permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00558};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC       {ECO:0000255|HAMAP-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
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00558}.
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DR   EMBL; CR522870; CAG35013.1; -; Genomic_DNA.
DR   RefSeq; YP_064020.1; NC_006138.1.
DR   ProteinModelPortal; Q6ARL2; -.
DR   STRING; 177439.DP0284; -.
DR   EnsemblBacteria; CAG35013; CAG35013; DP0284.
DR   GeneID; 2945074; -.
DR   KEGG; dps:DP0284; -.
DR   PATRIC; 21710115; VBIDesPsy67261_0312.
DR   eggNOG; COG0045; -.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; QVILINI; -.
DR   OrthoDB; EOG644ZT0; -.
DR   BioCyc; DPSY177439:GJW5-287-MONOMER; -.
DR   UniPathway; UPA00223; UER00999.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 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; IPR013816; ATP_grasp_subdomain_2.
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;
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    386       Succinyl-CoA ligase [ADP-forming] subunit
FT                                beta.
FT                                /FTId=PRO_1000082071.
FT   DOMAIN        9    243       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00558}.
FT   NP_BIND      35    107       ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       196    196       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
FT   METAL       198    198       Magnesium or manganese.
FT                                {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ   SEQUENCE   386 AA;  41828 MW;  1298E942D8207210 CRC64;
     MKIHEYQAKQ LFRKYSIPVP EGLLCTNLQE VKTALKSLQL PIAVKAQIHA GGRGKGGGVK
     LGKTATEVVQ YADDILGMSL VTAQTGPSGR TVSKILLEEG VSIARELYLS ILVDRERACI
     TIIACQDGGM NIEEVAASTP ERIGKIHINP LIGPRSYHIN QAREWLNIAQ EQARAFSLFI
     HALYKLFLDY DCSMVEINPL IITEDNQLIA LDAKVDTDSN ALFRQRELQK MHDPAEDDPA
     EAEAAKFNLN YIKLSGNVGN MVNGAGLAMA TMDIIKRAGA EPANFLDVGG SADAERIENG
     FRIILADTNV KAILINIFGG ILRCDILAQG VVQAAAKVSL QVPVVIRMEG TNVKEGREIL
     AKSGLSLINA TDLNDAAEKI STLLTD
//
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