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NORV_PECAS
ID   NORV_PECAS              Reviewed;         509 AA.
AC   Q6D8S0;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
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}; OrderedLocusNames=ECA0902;
OS   Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS   carotovora subsp. atroseptica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=218491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRI 1043 / ATCC BAA-672;
RX   PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA   Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA   Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA   Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA   Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA   Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA   Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT   "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT   subsp. atroseptica and characterization of virulence factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG73814.1; -; Genomic_DNA.
DR   RefSeq; WP_011092504.1; NC_004547.2.
DR   AlphaFoldDB; Q6D8S0; -.
DR   SMR; Q6D8S0; -.
DR   STRING; 218491.ECA0902; -.
DR   EnsemblBacteria; CAG73814; CAG73814; ECA0902.
DR   KEGG; eca:ECA0902; -.
DR   PATRIC; fig|218491.5.peg.906; -.
DR   eggNOG; COG0426; Bacteria.
DR   eggNOG; COG1773; Bacteria.
DR   HOGENOM; CLU_017490_0_1_6; -.
DR   OMA; HVKNNIH; -.
DR   OrthoDB; 1149616at2; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000007966; 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; IPR024935; Rubredoxin_dom.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF00301; Rubredoxin; 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..509
FT                   /note="Anaerobic nitric oxide reductase flavorubredoxin"
FT                   /id="PRO_0000305591"
FT   DOMAIN          254..393
FT                   /note="Flavodoxin-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   DOMAIN          457..508
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         462
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         465
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         495
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT   BINDING         498
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
SQ   SEQUENCE   509 AA;  57202 MW;  82A5D7E0662FE4C5 CRC64;
     MTIHVKNNIH WVGQRDWEVR DFHGTEYKTL QGSSYNSYLI REEKTVLIDT VDHKFSREFV
     QNLMAEVDLN TIDYIVINHA EEDHAGALSE LMARIPNTPI YCTYNAIDSI TGHHHHPEWN
     FHTVKTGDTL DIGNGKQLIF IETPMLHWPD SMMTYMTEDA VLFSNDAFGQ HYCDEHLFND
     EVDQTELFEQ CQRYFANILT PFSRLVTAKI HEVLGFNLPL SMVATSHGVV WRDDPAQIIH
     LYLKWADSYQ EDRITLFYDT MSNNTRMMAD AIAQGINDVD PGVAVKIYNV ARHDKNEILT
     QVFRSKGVLV GSSTMNNVMM PKVAAMLEEI TGLRFQNKKA SAFGSYGWNG GAVDRVQTRL
     MDAGFETTLA LKTKWRPDGS ALEVCREHGR EIARQWALHP LDNTPARRVI SPVKPAATAP
     QVTTAAQPMS ASAESACGCN EVAAPQSATQ PTVQSESGCM QCSVCQWIYD PALGEPMQDV
     TPGTMWSDVP DSFLCPECGL GKDVFNPIR
 
 
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