ID A0A0F7H9Y7_SERFO Unreviewed; 489 AA.
AC A0A0F7H9Y7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Anaerobic nitric oxide reductase flavorubredoxin {ECO:0000256|HAMAP-Rule:MF_01312};
DE Short=FlRd {ECO:0000256|HAMAP-Rule:MF_01312};
DE Short=FlavoRb {ECO:0000256|HAMAP-Rule:MF_01312};
GN Name=norV {ECO:0000256|HAMAP-Rule:MF_01312};
GN Synonyms=flrD {ECO:0000256|HAMAP-Rule:MF_01312};
GN ORFNames=WN53_10070 {ECO:0000313|EMBL:AKG69421.1};
OS Serratia fonticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG69421.1, ECO:0000313|Proteomes:UP000034699};
RN [1] {ECO:0000313|EMBL:AKG69421.1, ECO:0000313|Proteomes:UP000034699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG69421.1,
RC ECO:0000313|Proteomes:UP000034699};
RA Chan K.-G., Ee R.;
RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL Submitted (APR-2015) 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:0000256|HAMAP-
CC Rule:MF_01312}.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01312};
CC Note=Binds 1 FMN per monomer. {ECO:0000256|HAMAP-Rule:MF_01312};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01312};
CC Note=Binds 3 Fe cations per monomer. {ECO:0000256|HAMAP-Rule:MF_01312};
CC -!- PATHWAY: Nitrogen metabolism; nitric oxide reduction.
CC {ECO:0000256|HAMAP-Rule:MF_01312}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01312}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01312}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc metallo-
CC hydrolase group 3 family. {ECO:0000256|ARBA:ARBA00007121}.
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DR EMBL; CP011254; AKG69421.1; -; Genomic_DNA.
DR RefSeq; WP_024484755.1; NZ_CP011254.1.
DR AlphaFoldDB; A0A0F7H9Y7; -.
DR GeneID; 30320509; -.
DR KEGG; sfw:WN53_10070; -.
DR PATRIC; fig|47917.8.peg.2080; -.
DR UniPathway; UPA00638; -.
DR Proteomes; UP000034699; 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; cd07709; flavodiiron_proteins_MBL-fold; 1.
DR CDD; cd00730; rubredoxin; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 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; IPR045761; ODP_dom.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR024934; Rubredoxin-like_dom.
DR InterPro; IPR016440; Rubredoxin-O_OxRdtase.
DR InterPro; IPR024935; Rubredoxin_dom.
DR PANTHER; PTHR43717; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 1.
DR PANTHER; PTHR43717:SF1; ANAEROBIC NITRIC OXIDE REDUCTASE FLAVORUBREDOXIN; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF19583; ODP; 1.
DR Pfam; PF00301; Rubredoxin; 1.
DR PIRSF; PIRSF005243; ROO; 1.
DR PRINTS; PR00163; RUBREDOXIN.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR SUPFAM; SSF57802; Rubredoxin-like; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01312};
KW Electron transport {ECO:0000256|HAMAP-Rule:MF_01312};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01312};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01312};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01312};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01312}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01312};
KW Reference proteome {ECO:0000313|Proteomes:UP000034699};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01312}.
FT DOMAIN 254..393
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 433..484
FT /note="Rubredoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50903"
FT REGION 30..210
FT /note="Zinc metallo-hydrolase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT REGION 401..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 83
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 147
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 166
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 227
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 438
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 441
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 471
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
FT BINDING 474
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01312"
SQ SEQUENCE 489 AA; 55148 MW; 9B77F8312060C803 CRC64;
MAIQVKNNIQ WVGQRDWEVR DFHGTEYKTL KGSSYNSYLI REEKTVLIDT VDHKFSREFV
QNLSAEIDLQ TLDYIIINHA EEDHAGALSE LMVQIPNTPI YCTENGIDSI NGHHHHPEWN
FHVVHTGDSL DIGNGKQLIF VETPMLHWPD SMMTYITGDA VLFSNDAFGQ HYCDEHLFND
EVDQNELFEQ CQRYYANILT PFSRLVTPKI TEILGFNLPV DMIATSHGVV WRDNPTQIVQ
RYLEWAADYQ EDRITIFYDT MSNNTRMMAD AIAQGINEID ARVAVKIFNV ARHDKNEILT
NVFRSKGILV GSSTMNNVMM PKVAGLLEEI TGLRFRNKKA SAFGSYGWNG GAVDRIQTRL
MDSGFETTLA LKAKWRPDGD TLEICRQHGR DIARQWAISP LPAGKTVSTD TPPQAPLAST
TPAPLSTESA DLGPSMQCSV CLWVYDPQQG EPMQDVAPGT AWQNVPDDFL CPKCAMGKEV
FDALKPEAK
//
