ID O07463_RHOPL Unreviewed; 277 AA. AC O07463; DT 01-JUL-1997, integrated into UniProtKB/TrEMBL. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 64. DE SubName: Full=Benzoyl-CoA reductase subunit {ECO:0000313|EMBL:AAC23928.1}; GN Name=badG {ECO:0000313|EMBL:AAC23928.1}; OS Rhodopseudomonas palustris. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=1076 {ECO:0000313|EMBL:AAC23928.1}; RN [1] {ECO:0000313|EMBL:AAC23928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGA009 {ECO:0000313|EMBL:AAC23928.1}; RX PubMed=9177244; DOI=10.1073/pnas.94.12.6484; RA Egland P.G., Pelletier D.A., Dispensa M., Gibson J., Harwood C.S.; RT "A cluster of bacterial genes for anaerobic benzene ring biodegradation."; RL Proc. Natl. Acad. Sci. U.S.A. 94:6484-6489(1997). RN [2] {ECO:0000313|EMBL:AAC23928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGA009 {ECO:0000313|EMBL:AAC23928.1}; RX PubMed=9573182; RA Pelletier D.A., Harwood C.S.; RT "2-Ketocyclohexanecarboxyl coenzyme A hydrolase, the ring cleavage enzyme RT required for anaerobic benzoate degradation by Rhodopseudomonas RT palustris."; RL J. Bacteriol. 180:2330-2336(1998). RN [3] {ECO:0000313|EMBL:AAC23928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CGA009 {ECO:0000313|EMBL:AAC23928.1}; RA Egland P.G., Pelletier D.A., Dispensa M., Gibson J., Harwood C.S.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|ARBA:ARBA00001966}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U75363; AAC23928.1; -; Genomic_DNA. DR PIR; T51770; T51770. DR AlphaFoldDB; O07463; -. DR BioCyc; MetaCyc:MONOMER-891; -. DR BRENDA; 1.3.7.8; 5412. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR002731; ATPase_BadF. DR InterPro; IPR043129; ATPase_NBD. DR InterPro; IPR011956; Benzoyl_CoA_Rdtase_D. DR InterPro; IPR008275; CoA_E_activase_dom. DR NCBIfam; TIGR02261; benz_CoA_red_D; 1. DR NCBIfam; TIGR00241; CoA_E_activ; 1. DR PANTHER; PTHR32329; BIFUNCTIONAL PROTEIN [INCLUDES 2-HYDROXYACYL-COA DEHYDRATASE (N-TER) AND ITS ACTIVATOR DOMAIN (C_TERM)-RELATED; 1. DR PANTHER; PTHR32329:SF2; BIFUNCTIONAL PROTEIN [INCLUDES 2-HYDROXYACYL-COA DEHYDRATASE (N-TER) AND ITS ACTIVATOR DOMAIN (C_TERM)-RELATED; 1. DR Pfam; PF01869; BcrAD_BadFG; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 1. PE 4: Predicted; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}. FT DOMAIN 6..263 FT /note="ATPase BadF/BadG/BcrA/BcrD type" FT /evidence="ECO:0000259|Pfam:PF01869" SQ SEQUENCE 277 AA; 29616 MW; B570491396918523 CRC64; MTITSGIDVG TGAIKVVAFE VDGDQERCLA KRVERVRQRD PMKLSGDIYD DMLKETGLAR ADVAYCSTTG EGEALTFHTG HFYSMTTHAR GAIYLNPASR AVLDTGALHV RAIRMDERGK VLAYKMTSQC ASGSGQFLEN IARYLGIAQD EIGSLSQRAD NPEKVSGICA VLAETDVINM VSRGISSPNI LRGIHESMAD RLAKLLKTLG SLDGTVQMTG GLALDTGLVE AMKDAVVKAK VEVAIESHPD SIYAGAIGAA LWGAFRHKRL ADMARAA //