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 29-MAY-2013, entry version 71.
DE RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta;
DE EC=6.2.1.5;
DE AltName: Full=Succinyl-CoA synthetase subunit beta;
DE Short=SCS-beta;
GN Name=sucC; 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.
CC -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC similarity).
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC succinate from succinyl-CoA (ligase route): step 1/1.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits (By
CC similarity).
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC subunit family.
CC -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; VANANEM; -.
DR BioCyc; DPSY177439:GJW5-287-MONOMER; -.
DR UniPathway; UPA00223; UER00999.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:HAMAP.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA: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; CoA_ligase; 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; 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.
FT NP_BIND 35 107 ATP (By similarity).
FT METAL 196 196 Magnesium or manganese (By similarity).
FT METAL 198 198 Magnesium or manganese (By similarity).
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
//
