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Database: UniProt
Entry: A9IKE3
LinkDB: A9IKE3
Original site: A9IKE3 
ID   SUCC_BORPD              Reviewed;         386 AA.
AC   A9IKE3;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-SEP-2014, entry version 50.
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=Bpet2061;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P.,
RA   Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J.,
RA   Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N.,
RA   Larisch C., Link S., Linke B., Meyer F., Mormann S., Nakunst D.,
RA   Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J.,
RA   Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B.,
RA   Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the
RT   metabolic versatility of environmental bacteria and virulence traits
RT   of pathogenic Bordetellae.";
RL   BMC Genomics 9:449-449(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.
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DR   EMBL; AM902716; CAP42401.1; -; Genomic_DNA.
DR   RefSeq; WP_012248977.1; NC_010170.1.
DR   RefSeq; YP_001630670.1; NC_010170.1.
DR   ProteinModelPortal; A9IKE3; -.
DR   SMR; A9IKE3; 1-385.
DR   STRING; 340100.Bpet2061; -.
DR   EnsemblBacteria; CAP42401; CAP42401; Bpet2061.
DR   GeneID; 5818073; -.
DR   KEGG; bpt:Bpet2061; -.
DR   PATRIC; 21165591; VBIBorPet31633_2058.
DR   eggNOG; COG0045; -.
DR   HOGENOM; HOG000007059; -.
DR   KO; K01903; -.
DR   OMA; AAGRICK; -.
DR   OrthoDB; EOG644ZT0; -.
DR   BioCyc; BPET340100:GJBO-2087-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; Tricarboxylic acid cycle.
FT   CHAIN         1    386       Succinyl-CoA ligase [ADP-forming] subunit
FT                                beta.
FT                                /FTId=PRO_1000129163.
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;  41113 MW;  C97F128821DE2947 CRC64;
     MKIHEYQGKE LLKQFGVPVP RGIPAFSVDE AVAAAEKLGG PVWVVKAQIH AGGRGKGGGV
     KLARSLDDVR KLASEILGMQ LVTHQTGPEG QKVNRLYIED GADIQKEYYV SLVTDRATQK
     VAIIASSEGG MDIEEVAHST PEKIITEYID PLTGLQAEQA KKVAESIGLS GGSADQAADV
     FQKLYTCYMD TDASLVEINP LNCDSKGNII ALDAKFNFDS NALFRHPEIV AYRDLDEEDP
     AEIEASKFDL AYIQLDGNIG CLVNGAGLAM ATMDTIKLFG GEPANFLDVG GGATAEKVTE
     AFKIMLKNKG VKAILVNIFG GIMRCDVIAE GVITACKAVN LNVPLVVRMK GTNEELGKKM
     LADSGLPIIS ADTMAEAATR VVAAVK
//
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