NRFB_HAEIN
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 03-AUG-2022, entry version 112.
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; Proteobacteria; 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}.
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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 OMA; EQNQVCF; -.
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 InterPro; IPR017564; Cyt_c_NO2Rdtase_pentahaem-su.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR SUPFAM; SSF48695; SSF48695; 1.
DR TIGRFAMs; TIGR03146; cyt_nit_nrfB; 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
