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NORV_KLEP7
ID   NORV_KLEP7              Reviewed;         482 AA.
AC   A6TCX5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=KPN78578_29850; ORFNames=KPN_03045;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR78446.1; -; Genomic_DNA.
DR   RefSeq; WP_015958870.1; NC_009648.1.
DR   AlphaFoldDB; A6TCX5; -.
DR   SMR; A6TCX5; -.
DR   STRING; 272620.KPN_03045; -.
DR   EnsemblBacteria; ABR78446; ABR78446; KPN_03045.
DR   KEGG; kpn:KPN_03045; -.
DR   HOGENOM; CLU_017490_0_1_6; -.
DR   OMA; HVKNNIH; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000000265; Chromosome.
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; Reference proteome; Transport.
FT   CHAIN           1..482
FT                   /note="Anaerobic nitric oxide reductase flavorubredoxin"
FT                   /id="PRO_0000341310"
FT   DOMAIN          254..393
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   DOMAIN          426..477
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         431
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         434
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         464
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         467
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
SQ   SEQUENCE   482 AA;  54390 MW;  1F4ABFE1B412FF2F CRC64;
     MSIVVKNNIL WVGQRDWEVR DFHGTEYKTL RGSSYNSYLI REEKNVLIDT VDHKFSREFV
     QNLRREIDLA DLDYIVINHA EEDHAGALTE LMMQIPDTPI YCTANAIDSI NGHHHHPEWN
     FHVVKTGDTL DIGNGKQLIF VETPMLHWPD SMMTYLTGDA VLFSNDAFGQ HYCDEHLFND
     EVDQTELYEQ CQRYYANILT PFSRLVTPKI TEILGFNLPV EMIATSHGVV WRDNPTQIVE
     KYLEWAADYQ EDRITIFYDT MSNNTRMMAD AIAQGITEVD PQVAVKIFNV ARSDKNDILT
     NVFRSKGVLV GTSTMNNVMM PKIAGLVEEM TGLRFRNKRA SAFGSHGWSG GAVDRLSTRL
     QDAGFEMSLS LKAKWRPDID ALELCRQHGR DIARQWALSP LPVAEAATTP EPQDCACAAA
     AAADLGPMMQ CSVCQWVYDP AKGEPNQDVQ PGTPWSEVPD NFLCPECSLG KDVFDVLATE
     AK
 
 
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