ID FNR_VIBCH Reviewed; 250 AA. AC P0C6D0; Q9KS27; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 80. DE RecName: Full=Fumarate and nitrate reduction regulatory protein; GN Name=fnr; OrderedLocusNames=VC_1434; OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=243277; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39315 / El Tor Inaba N16961; RX PubMed=10952301; DOI=10.1038/35020000; RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A., RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.; RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio RT cholerae."; RL Nature 406:477-483(2000). CC -!- FUNCTION: Global transcription factor that controls the expression of CC over 100 target genes in response to anoxia. It facilitates the CC adaptation to anaerobic growth conditions by regulating the expression CC of gene products that are involved in anaerobic energy metabolism. When CC the terminal electron acceptor, O(2), is no longer available, it CC represses the synthesis of enzymes involved in aerobic respiration and CC increases the synthesis of enzymes required for anaerobic respiration CC (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. 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; AE003852; AAF94591.1; -; Genomic_DNA. DR PIR; F82199; F82199. DR RefSeq; NP_231077.1; NC_002505.1. DR RefSeq; WP_000622582.1; NZ_LT906614.1. DR AlphaFoldDB; P0C6D0; -. DR SMR; P0C6D0; -. DR STRING; 243277.VC_1434; -. DR DNASU; 2614066; -. DR EnsemblBacteria; AAF94591; AAF94591; VC_1434. DR GeneID; 69719895; -. DR KEGG; vch:VC_1434; -. DR PATRIC; fig|243277.26.peg.1364; -. DR eggNOG; COG0664; Bacteria. DR HOGENOM; CLU_075053_0_2_6; -. DR Proteomes; UP000000584; Chromosome 1. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd00038; CAP_ED; 1. DR CDD; cd00092; HTH_CRP; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR018490; cNMP-bd_dom_sf. DR InterPro; IPR012318; HTH_CRP. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1. DR PANTHER; PTHR24567:SF75; FUMARATE AND NITRATE REDUCTION REGULATORY PROTEIN; 1. DR Pfam; PF00027; cNMP_binding; 1. DR Pfam; PF13545; HTH_Crp_2; 1. DR PRINTS; PR00034; HTHCRP. DR SMART; SM00100; cNMP; 1. DR SMART; SM00419; HTH_CRP; 1. DR SUPFAM; SSF51206; cAMP-binding domain-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. DR PROSITE; PS00042; HTH_CRP_1; 1. DR PROSITE; PS51063; HTH_CRP_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Activator; Cytoplasm; DNA-binding; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1..250 FT /note="Fumarate and nitrate reduction regulatory protein" FT /id="PRO_0000100170" FT DOMAIN 164..237 FT /note="HTH crp-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387" FT DNA_BIND 200..219 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387" FT REGION 23..32 FT /note="Essential for the oxygen-regulated activity" FT /evidence="ECO:0000250" FT REGION 50..53 FT /note="Activating region 2A" FT /evidence="ECO:0000255" FT REGION 63..64 FT /note="Activating region 3A" FT /evidence="ECO:0000255" FT REGION 74..78 FT /note="Activating region 1A" FT /evidence="ECO:0000255" FT REGION 84 FT /note="Activating region 3B" FT /evidence="ECO:0000255" FT REGION 88..90 FT /note="Activating region 3C" FT /evidence="ECO:0000255" FT REGION 115 FT /note="Activating region 3D" FT /evidence="ECO:0000255" FT REGION 119..124 FT /note="Activating region 1B" FT /evidence="ECO:0000255" FT REGION 126..127 FT /note="Activating region 2B" FT /evidence="ECO:0000255" FT REGION 130..131 FT /note="Activating region 2C" FT /evidence="ECO:0000255" FT REGION 143..162 FT /note="Dimerization" FT /evidence="ECO:0000255" FT REGION 184..194 FT /note="Activating region 1C" FT /evidence="ECO:0000255" FT BINDING 20 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT BINDING 23 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT BINDING 29 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" FT BINDING 122 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255" SQ SEQUENCE 250 AA; 28071 MW; A3E3ED036BBBC490 CRC64; MISEKPAAKR IQSGGCAIHC QDCSISQLCI PFTLNESELD QLDQIIERKK PIQKGQELFK AGDELRSLYA IRSGTIKSYT ITEQGDEQIT AFHLAGDLVG FDAITGDQHP SFAQALETSM VCEIPYEILD DLSGKMPKLR QQIMRLMSNE IKGDQEMILL LSKKNAEERL AAFLYNLSTR FSQRGFSPRE FRLTMTRGDI GNYLGLTVET ISRLLGRFQK SEILSVKGKY ITILNHAELM ELAGVSKESK //