UniProt: A0A0A7RZE6

Database: UniProt
Entry: A0A0A7RZE6_FRIPE

LinkDB:  A0A0A7RZE6_FRIPE 
Original site:  A0A0A7RZE6_FRIPE

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (19)   
   InterPro (13)   
   Pfam (5)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (31)   

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ID   A0A0A7RZE6_FRIPE        Unreviewed;       840 AA.
AC   A0A0A7RZE6;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Assimilatory nitrite reductase (NAD(P)H) large subunit {ECO:0000313|EMBL:AJA43957.1};
DE            EC=1.7.1.4 {ECO:0000313|EMBL:AJA43957.1};
GN   ORFNames=FPB0191_00091 {ECO:0000313|EMBL:AJA43957.1};
OS   Frischella perrara.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae;
OC   Frischella.
OX   NCBI_TaxID=1267021 {ECO:0000313|EMBL:AJA43957.1, ECO:0000313|Proteomes:UP000030901};
RN   [1] {ECO:0000313|EMBL:AJA43957.1, ECO:0000313|Proteomes:UP000030901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEB0191 {ECO:0000313|EMBL:AJA43957.1,
RC   ECO:0000313|Proteomes:UP000030901};
RX   PubMed=25527542;
RA   Engel P., Vizcaino M.I., Crawford J.M.;
RT   "Gut symbionts from distinct hosts exhibit genotoxic activity via divergent
RT   colibactin biosynthetic pathways.";
RL   Appl. Environ. Microbiol. 0:0-0(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRNR:PIRNR037149};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000256|ARBA:ARBA00001929};
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC       {ECO:0000256|ARBA:ARBA00005096}.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000256|ARBA:ARBA00010429}.
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DR   EMBL; CP009056; AJA43957.1; -; Genomic_DNA.
DR   RefSeq; WP_039103240.1; NZ_QGTI01000006.1.
DR   AlphaFoldDB; A0A0A7RZE6; -.
DR   STRING; 1267021.FPB0191_00091; -.
DR   GeneID; 78458553; -.
DR   KEGG; fpp:FPB0191_00091; -.
DR   HOGENOM; CLU_003291_0_0_6; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000030901; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd19943; NirB_Fer2_BFD-like_1; 1.
DR   CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.90.480.20; -; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR   InterPro; IPR012744; Nitri_red_NirB.
DR   InterPro; IPR017121; Nitrite_Rdtase_lsu.
DR   InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   NCBIfam; TIGR02374; nitri_red_nirB; 1.
DR   PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF18267; Rubredoxin_C; 1.
DR   PIRSF; PIRSF037149; NirB; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR037149};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR037149}; Heme {ECO:0000256|ARBA:ARBA00022617};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW   ECO:0000256|PIRNR:PIRNR037149};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AJA43957.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030901}.
FT   DOMAIN          5..285
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          319..387
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          421..468
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          557..618
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          630..768
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   840 AA;  92145 MW;  4227EF88450EA766 CRC64;
     MNKTSLVIIG NGMVGHRFVE EIIDKNLSDQ FEITIFCEEP RLAYDRVHLS SYFSDNNAQA
     LSLVSEGLYQ TNYITVFMGE RAVSINRQTK EVCSQTGRVV SYDKLIIATG SYPWVPPIKG
     AQGKNCFVYR TIEDLDAIRA CASQSRKGAV VGGGLLGLEA AGAVKNLGME THVIEFAPVL
     MAEQLDALGG EQLRRKIEDM GVNVHISKNT LEIMDTLDGK VMQFADGSSL DVDFIVFSTG
     IRPNDKLARD CELAIADRGG IIINNYCQTS DPNIYAIGEC ASWQGRVFGL VAPGYKMAQV
     VLGHLMGENI QFSGADMSAK LKLLGVDVGS IGDAKGKTTN CQSYIYLDET IPIYKKLVVS
     ADNKQLLGAV LVGDTSDYGS LLQLMLNNMP LPEHPDTLIL PTYVGEKPAL GADALPDSAQ
     ICSCFDISKA RIVEAIHAGC HTVAAIKAET KAGTGCGGCL PLVTQILNSE LAKQGIEVSH
     ALCKHFNYSR QELFHLVRIE GLTSFEQVIK KHGNGYGCEI CKPTIGSILA SCWNSYILKP
     DLVPLQDSND IFLGNIQKNG TYSIIPRSAG GEITPEGLIA IGKIAQKYHL YSKITGSQRI
     GLFGAQKDDL PVIWQELINA GFESGHAYAK ALRMAKTCVG STWCRFGVGD SVGLGVELEN
     RYKGIRAPHK FKLGVSGCTR ECAEAQGKDI GVIATEKGWN LYVCGNGGMK PRHADLLAAD
     LDKETLIRYL DRFIMFYIRT ADKLQRTSVW LENLEGGINY LRSVIIEDKL GVNAELENEM
     ARIRKLVVCE WKETVTQPDK QNRFAHFINS QQRDDNVVFV PEREQHRPAT FEERKAILGE
//

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