ID SUCC_WOLPP Reviewed; 386 AA.
AC B3CME9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 01-MAY-2013, entry version 44.
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=WP0961;
OS Wolbachia pipientis subsp. Culex pipiens (strain wPip).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=570417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wPip;
RX PubMed=18550617; DOI=10.1093/molbev/msn133;
RA Klasson L., Walker T., Sebaihia M., Sanders M.J., Quail M.A., Lord A.,
RA Sanders S., Earl J., O'Neill S.L., Thomson N., Sinkins S.P.,
RA Parkhill J.;
RT "Genome evolution of Wolbachia strain wPip from the Culex pipiens
RT group.";
RL Mol. Biol. Evol. 25:1877-1887(2008).
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; AM999887; CAQ55069.1; -; Genomic_DNA.
DR RefSeq; YP_001975714.1; NC_010981.1.
DR STRING; 570417.WPa_0961; -.
DR PRIDE; B3CME9; -.
DR EnsemblBacteria; CAQ55069; CAQ55069; WP0961.
DR GeneID; 6384927; -.
DR KEGG; wpi:WPa_0961; -.
DR PATRIC; 24027618; VBIWolEnd95846_1043.
DR eggNOG; COG0045; -.
DR KO; K01903; -.
DR OMA; QPVTKIL; -.
DR ProtClustDB; PRK00696; -.
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_1000129237.
FT DOMAIN 9 244 ATP-grasp.
FT NP_BIND 35 108 ATP (By similarity).
FT METAL 197 197 Magnesium or manganese (By similarity).
FT METAL 199 199 Magnesium or manganese (By similarity).
SQ SEQUENCE 386 AA; 42052 MW; 15BA75830C362617 CRC64;
MNIHEYQAKE ILHKFNVPVP KGFVATSAEG VETQINQLKS DVFVVKAQIH AGGRGKAGGV
KLAKSVEEAQ QFVKNMLGIT LVTHQTGPSG QQVRRIYIEE GSSIKKEYYL SLVVDPKLSR
LVFIFSSEGG MDIEEVAKNS PTKIVKFDID PATGFTNLDN SKLANNFNLN SEQIERITNI
AKNIYDAFIT TDASQIEINP LVETNSGDFV ALDAKINFDD NALYRHPEIV QLRDYDEEVK
EEIEASKHGL SYIKMDGNIG CMVNGAGLAM ATMDIIKYYG AEPANFLDVG GGASKETVTE
AFKIILSDSN VKGILVNIFG GIMRCDIIAS GIVAAAKEMS IKVPLVVRLS GTNFEEGKKI
LEESGLNIIA ADELGDAAQK IVKEVK
//
