ID NRFB_HAEIN Reviewed; 226 AA. AC P45016; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=Cytochrome c-type protein NrfB; DE Flags: Precursor; GN Name=nrfB; OrderedLocusNames=HI_1068; OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=71421; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd; RX PubMed=7542800; DOI=10.1126/science.7542800; RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F., RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.; RT "Whole-genome random sequencing and assembly of Haemophilus influenzae RT Rd."; RL Science 269:496-512(1995). CC -!- FUNCTION: Plays a role in nitrite reduction. {ECO:0000250}. CC -!- PATHWAY: Energy metabolism; nitrogen metabolism. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. CC -!- PTM: Binds 5 heme groups per subunit. {ECO:0000250}. 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; L42023; AAC22726.1; -; Genomic_DNA. DR PIR; B64181; B64181. DR RefSeq; NP_439226.2; NC_000907.1. DR AlphaFoldDB; P45016; -. DR SMR; P45016; -. DR STRING; 71421.HI_1068; -. DR EnsemblBacteria; AAC22726; AAC22726; HI_1068. DR KEGG; hin:HI_1068; -. DR PATRIC; fig|71421.8.peg.1112; -. DR eggNOG; COG3303; Bacteria. DR HOGENOM; CLU_104606_0_0_6; -. DR OrthoDB; 6398708at2; -. DR PhylomeDB; P45016; -. DR UniPathway; UPA00045; -. DR Proteomes; UP000000579; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.10.10; Cytochrome C3; 1. DR InterPro; IPR017564; Cyt_c_NrfB. DR InterPro; IPR036280; Multihaem_cyt_sf. DR NCBIfam; TIGR03146; cyt_nit_nrfB; 1. DR SUPFAM; SSF48695; Multiheme cytochromes; 1. DR PROSITE; PS51008; MULTIHEME_CYTC; 1. PE 3: Inferred from homology; KW Electron transport; Heme; Iron; Metal-binding; Periplasm; KW Reference proteome; Signal; Transport. FT SIGNAL 1..39 FT /evidence="ECO:0000255" FT CHAIN 40..226 FT /note="Cytochrome c-type protein NrfB" FT /id="PRO_0000006586" FT BINDING 65 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 68 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 69 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" FT BINDING 110 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 113 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" FT BINDING 152 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="3" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 155 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="3" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 156 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="3" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" FT BINDING 177 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="4" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 180 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="4" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 181 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="4" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" FT BINDING 202 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="5" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 205 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="5" FT /note="covalent" FT /evidence="ECO:0000250" FT BINDING 206 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="5" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250" SQ SEQUENCE 226 AA; 25664 MW; 959F2DCEA668030A CRC64; MIFKVKFEVT QMILTSLINK SAKALVIVAF VAAPFLAHAD DAQKPAVHVT YEPQLDNQRD PNQYCAKCHK FDKIDKNQTL DQSGGELHFG KFHGAHLDKK NPNNGKAITC VSCHGNISEN HRRGAKDVMR FEGDIFGNKK PMYSVQEQNQ VCFACHQPDK LREKLWAHDV HAMKLPCASC HTLHPKEDAM KGIQPKQRVK LCVDCHGEQQ KRKAEQDKLI EQKDKL //