NORV_VIBVU
ID NORV_VIBVU Reviewed; 494 AA.
AC Q8D4F8;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Anaerobic nitric oxide reductase flavorubredoxin {ECO:0000255|HAMAP-Rule:MF_01312};
DE Short=FlRd {ECO:0000255|HAMAP-Rule:MF_01312};
DE Short=FlavoRb {ECO:0000255|HAMAP-Rule:MF_01312};
GN Name=norV {ECO:0000255|HAMAP-Rule:MF_01312};
GN Synonyms=flrD {ECO:0000255|HAMAP-Rule:MF_01312};
GN OrderedLocusNames=VV2_1343;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Anaerobic nitric oxide reductase; uses NADH to detoxify
CC nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has
CC at least 2 reductase partners, only one of which (NorW, flavorubredoxin
CC reductase) has been identified. NO probably binds to the di-iron
CC center; electrons enter from the NorW at rubredoxin and are transferred
CC sequentially to the FMN center and the di-iron center. Also able to
CC function as an aerobic oxygen reductase. {ECO:0000255|HAMAP-
CC Rule:MF_01312}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01312};
CC Note=Binds 3 Fe cations per monomer. {ECO:0000255|HAMAP-Rule:MF_01312};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01312};
CC Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_01312};
CC -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC {ECO:0000255|HAMAP-Rule:MF_01312}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01312}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01312}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000255|HAMAP-Rule:MF_01312}.
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DR EMBL; AE016796; AAO08230.1; -; Genomic_DNA.
DR RefSeq; WP_011082226.1; NC_004460.2.
DR AlphaFoldDB; Q8D4F8; -.
DR SMR; Q8D4F8; -.
DR EnsemblBacteria; AAO08230; AAO08230; VV2_1343.
DR GeneID; 66966720; -.
DR KEGG; vvu:VV2_1343; -.
DR HOGENOM; CLU_017490_0_1_6; -.
DR OMA; HVKNNIH; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000002275; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016966; F:nitric oxide reductase activity; IEA:InterPro.
DR CDD; cd00730; rubredoxin; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01312; NorV; 1.
DR InterPro; IPR023957; Anaer_NO_rdtase_flvorubredoxin.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR016440; Rubredoxin-O_OxRdtase.
DR InterPro; IPR024935; Rubredoxin_dom.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF00301; Rubredoxin; 1.
DR PIRSF; PIRSF005243; ROO; 1.
DR PRINTS; PR00163; RUBREDOXIN.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Electron transport; Flavoprotein; FMN; Iron; Metal-binding;
KW Oxidoreductase; Transport.
FT CHAIN 1..494
FT /note="Anaerobic nitric oxide reductase flavorubredoxin"
FT /id="PRO_0000216791"
FT DOMAIN 254..393
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT DOMAIN 441..492
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT REGION 30..210
FT /note="Zinc metallo-hydrolase"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 260..264
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 342..369
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 446
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 449
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 479
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 482
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
SQ SEQUENCE 494 AA; 55610 MW; 9B15C5A1487C7C21 CRC64;
MTIHVKNNIH WVGQRDWEVQ DFHGTEYKMT KGTSYNSYLI REEKTVLIDT VDHRFSQQFI
QNLQMEIDLQ SIDFIVINHA EEDHSGALSA LMEKIPNTPI YCTEAAIDSI VGHHHHPEWN
FKTVKTGDSI DIGNGKQLVF VEAPMLHWPD SMMTYLTGDA VLFSNDAFGQ HYCDERLFND
EVDQAELMEQ CLRYYSNILT PFSALVTAKI QEVLSFNLPV DMIATSHGIV WRENPTQIIE
QYLAWANDYQ EDRITIFYDS MSNNTRMMAD AIAQGIHDVD PSVAVKVFNV SKQDKNEILA
NVFRSKGILV GSSTMNNVMM PKIAGMLEEI TGLRFKAKKA AAFGSYGWNG GAVDRIHARL
TDAGFETAIS LKTKWRPDGK AMRECREHGQ QIAKLWAVKD KSTLSTPVNA FQSATPIEGI
EAQQPLTETT PTADAAHSAD CQCMVCTVCN WVYDPAKGEP NQGIEVGTTW ADVPDYFLCP
ECHLGKDVFV EYQG
