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NORV_VIBVY
ID   NORV_VIBVY              Reviewed;         494 AA.
AC   Q7MFY8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=VVA0181;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
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; BA000038; BAC96207.1; -; Genomic_DNA.
DR   RefSeq; WP_011151604.1; NC_005140.1.
DR   AlphaFoldDB; Q7MFY8; -.
DR   SMR; Q7MFY8; -.
DR   EnsemblBacteria; BAC96207; BAC96207; BAC96207.
DR   KEGG; vvy:VVA0181; -.
DR   HOGENOM; CLU_017490_0_1_6; -.
DR   OMA; HVKNNIH; -.
DR   OrthoDB; 1149616at2; -.
DR   UniPathway; UPA00638; -.
DR   Proteomes; UP000002675; Chromosome II.
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..494
FT                   /note="Anaerobic nitric oxide reductase flavorubredoxin"
FT                   /id="PRO_0000305602"
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;  55609 MW;  3B15C141487C7F77 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
     QYLAWANNYQ 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
 
 
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