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 01-MAY-2013, entry version 45.
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; 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; TDRATQK; -.
DR ProtClustDB; PRK00696; -.
DR BioCyc; BPET340100:GJBO-2087-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_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
//
