UniProt: A0A0C5VH66

Database: UniProt
Entry: A0A0C5VH66_9GAMM

LinkDB:  A0A0C5VH66_9GAMM 
Original site:  A0A0C5VH66_9GAMM

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (20)   
   InterPro (14)   
   Pfam (5)   
   PROSITE (1)   
All databases (32)   

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ID   A0A0C5VH66_9GAMM        Unreviewed;       833 AA.
AC   A0A0C5VH66;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   28-JAN-2026, entry version 52.
DE   SubName: Full=NAD(P)H-nitrite reductase {ECO:0000313|EMBL:AJQ93987.1};
DE            EC=1.7.1.4 {ECO:0000313|EMBL:AJQ93987.1};
GN   ORFNames=YC6258_01943 {ECO:0000313|EMBL:AJQ93987.1};
OS   Gynuella sunshinyii YC6258.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Oceanospirillales; Saccharospirillaceae; Gynuella.
OX   NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ93987.1, ECO:0000313|Proteomes:UP000032266};
RN   [1] {ECO:0000313|EMBL:AJQ93987.1, ECO:0000313|Proteomes:UP000032266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6258 {ECO:0000313|EMBL:AJQ93987.1,
RC   ECO:0000313|Proteomes:UP000032266};
RA   Khan H., Chung E.J., Chung Y.R.;
RT   "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT   YC6258T gen. nov., sp. nov.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRNR:PIRNR037149};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037149-1};
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR037149-1};
CC   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000256|PIRSR:PIRSR037149-1};
CC       Note=Binds 1 siroheme per subunit. {ECO:0000256|PIRSR:PIRSR037149-1};
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; CP007142; AJQ93987.1; -; Genomic_DNA.
DR   RefSeq; WP_044616611.1; NZ_CP007142.1.
DR   AlphaFoldDB; A0A0C5VH66; -.
DR   STRING; 1445510.YC6258_01943; -.
DR   KEGG; gsn:YC6258_01943; -.
DR   PATRIC; fig|1445510.3.peg.1900; -.
DR   HOGENOM; CLU_003291_0_0_6; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000032266; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR   FunFam; 3.30.413.10:FF:000007; Nitrite reductase [NAD(P)H] large subunit; 1.
DR   FunFam; 3.50.50.60:FF:000033; Nitrite reductase [NAD(P)H], large subunit; 1.
DR   FunFam; 3.30.390.30:FF:000006; Nitrite reductase large subunit; 1.
DR   Gene3D; 3.30.390.30; -; 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; IPR052034; NasD-like.
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   NCBIfam; NF011565; PRK14989.1; 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   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRSR:PIRSR037149-1};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR037149};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR037149};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR037149-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR037149-1};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR037149-
KW   1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR037149-1};
KW   Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063,
KW   ECO:0000256|PIRNR:PIRNR037149};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AJQ93987.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032266}.
FT   DOMAIN          8..305
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          322..387
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          425..471
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          561..623
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          633..758
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
FT   BINDING         642
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
FT   BINDING         648
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
FT   BINDING         682
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
FT   BINDING         686
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
FT   BINDING         686
FT                   /ligand="siroheme"
FT                   /ligand_id="ChEBI:CHEBI:60052"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037149-1"
SQ   SEQUENCE   833 AA;  91382 MW;  18D8AEEE3E8837D6 CRC64;
     MNNFERKKLV VIGNGMVGHH LLETLADRQQ LSSFDITVFA DEPRLAYDRV HLSSYFSGST
     VDDLSLGSID QYQQWGITVR LNEQVTGIDT ETQEITSSSG FITHYDKLVL ATGSYPFTPP
     ITGKTDTNSL VYRTIEDLER IKSAAADSRI GVVIGGGLLG LEAAKALKDL GLETHVVEFS
     SRLMAIQLDE DGGNLLKQKI TALGVQVHTG KNTQSIGPGE QCKYRLNFAD DTVLETDLIL
     FSAGIRPRDE LARECGLAIG ERGGIVIDSN CMTSNPNIYA IGECALWNGR IFGLVAPGYK
     MAKVAAAHLT HQNDQFIGAD MSTKLKLLGV DVGSIGDAQG HSDGCINYRY LDEAAQSYRR
     IVVSADKKRL LGAVLVGDNS RYDTLLQYAL NGIELPAQPE SLILPLAEGS APTLGPGSLP
     ESATLCSCLN VTKGDIQAAI DAGAMSLTDV KNITKASSGC GGCAALLKNV VDHELAQRGV
     EINHSLCEHF SYTRQDLYNL VRVENIHSFD ELIDKHGNGL GCDICKPTVA SILASCWNEH
     IQIPRHVHLQ DTNDTFMANM QKNGTYSVVP RIAGGEITPA KLKVLAEVAE KYQLYTKITG
     GQRIDLFGAQ LHQLPLIWEE LIAAGFETGH AYGKAVRTVK SCVGSTWCRY GQQDSVGKAI
     EIEHRYKGLR APHKLKFAVS GCTRECAEAQ SKDIGIIATE NGWNLYVCGN GGMKPRHADL
     FATDLDDQTL IRYIDRILMF YVKTADRLQR TATWLDNLEG GLSYLQQVVI HDSLGICQSL
     EQQMQDTVDT YQCEWKSTIE NPELRKRFRT FVNNSGGDDR IVMIEERQQL RPA
//

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