ID SUCC_BORA1 Reviewed; 386 AA. AC Q2KYF7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 16-JUN-2009, entry version 28. 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=BAV2304; OS Bordetella avium (strain 197N). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Alcaligenaceae; Bordetella. OX NCBI_TaxID=360910; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16885469; DOI=10.1128/JB.01927-05; RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., RA King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., RA Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., RA Squares S., Woodward J., Parkhill J., Temple L.M.; RT "Comparison of the genome sequence of the poultry pathogen Bordetella RT avium with those of B. bronchiseptica, B. pertussis, and B. RT parapertussis reveals extensive diversity in surface structures RT associated with host interaction."; RL J. Bacteriol. 188:6002-6015(2006). 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 -!- 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; AM167904; CAJ49914.1; -; Genomic_DNA. DR RefSeq; YP_786818.1; -. DR GeneID; 6267778; -. DR GenomeReviews; AM167904_GR; BAV2304. DR KEGG; bav:BAV2304; -. DR NMPDR; fig|521.1.peg.133; -. DR HOGENOM; Q2KYF7; -. DR OMA; Q2KYF7; TDRATQK. DR GO; GO:0005524; F:ATP binding; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:HAMAP. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP. DR HAMAP; MF_00558; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type. 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 Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1. DR Gene3D; G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1. DR PANTHER; PTHR11815; CoA_lig_beta; 1. DR Pfam; PF08442; ATP-grasp_2; 1. DR Pfam; PF00549; Ligase_CoA; 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_1000082024. 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; 41137 MW; 023BAC2DEAC7A339 CRC64; MKIHEYQGKE LLKQFGVPVP RGIPAFSVEE AVAAAEKLGG PVWVVKAQIH AGGRGKGGGV KLARSLDEVR QLASQILGMQ LVTHQTGAQG QKVNRLYIED GADIQKEYYV SLVTDRGTQK VALIASSEGG MDIEEVAHST PEKIITEYID PIVGLTDAQA KKVADAIGMP ADSTAQAVDV FKKLYQCYMD TDASLVEINP LNRDSKGNII ALDAKFNFDS NALFRHPEIV AYRDLDEEDP AEIEASKFDL AYIQLDGNIG CLVNGAGLAM ATMDTIKLFG GEPANFLDVG GGATAEKVTE AFKIMLKNKG VKAILVNIFG GIMRCDVIAE GVISACKAVN LSVPLVVRMK GTNEELGKKM LAESGLPIIS ADTMAEAATK VVAAAK //