NORV_AERS4
ID NORV_AERS4 Reviewed; 521 AA.
AC A4STH4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=ASA_4272;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO92196.1; -; Genomic_DNA.
DR RefSeq; WP_005320624.1; NC_009348.1.
DR AlphaFoldDB; A4STH4; -.
DR SMR; A4STH4; -.
DR STRING; 382245.ASA_4272; -.
DR EnsemblBacteria; ABO92196; ABO92196; ASA_4272.
DR KEGG; asa:ASA_4272; -.
DR PATRIC; fig|382245.13.peg.4236; -.
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; UP000000225; 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; Transport.
FT CHAIN 1..521
FT /note="Anaerobic nitric oxide reductase flavorubredoxin"
FT /id="PRO_0000305590"
FT DOMAIN 254..393
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT DOMAIN 464..515
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 469
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 472
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 502
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
FT BINDING 505
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01312"
SQ SEQUENCE 521 AA; 57850 MW; 80603A12AD2741A5 CRC64;
MTIHVKNNIH WVGQRDWEVR DFHGTEYKTH KGTSYNSYLI REGKNVLIDT VDHKFSREFV
QNLAAEIDLA SIDVIVINHA EEDHAGALTE LMARIPGTPI YCTHNAIDSI TGHHHHPEWN
FHPVKTGDSL DIGNGKQLVF IETPMLHWPD SMMTYMTEDA VLFSNDAFGQ HYCDEHLFND
EVDQTELMEQ CQRYYANILT PFSPLVTAKI KEVLGFNLPV SMVATSHGIV WRDDPTQIIL
KYLEWADHYQ EDRITLFYDS MSNNTRMMAD AIAQGIHEVD PGVAVKIYNV ARHDKNEILT
QVFRSKGVLV GSSTMNNVMM PKVAGMLEEI TGLRFRNKRA SAFGSYGWTG GAVDRIQTRL
MDAGFDISIS LKAKWRPDGS ALALCREHGR QLARQWALHP LEAPCPIITT SAAAAPVVEA
GVVVEMSVPA SAGVVEVGVP AFSGAMELPV SRGVAPTTCE QDDDQPMLCT VCQWIYDPAL
GEPDQLVAPG TPWARVPDSF LCPGCGIGKE VFEPCAVEAC V
