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Database: UniProt
Entry: A0A418NHN1_9SPHN
LinkDB: A0A418NHN1_9SPHN
Original site: A0A418NHN1_9SPHN 
ID   A0A418NHN1_9SPHN        Unreviewed;       833 AA.
AC   A0A418NHN1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=NAD(P)/FAD-dependent oxidoreductase {ECO:0000313|EMBL:RIV78090.1};
GN   ORFNames=D2V04_09410 {ECO:0000313|EMBL:RIV78090.1};
OS   Pelagerythrobacter aerophilus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Pelagerythrobacter.
OX   NCBI_TaxID=2306995 {ECO:0000313|EMBL:RIV78090.1, ECO:0000313|Proteomes:UP000285092};
RN   [1] {ECO:0000313|EMBL:RIV78090.1, ECO:0000313|Proteomes:UP000285092}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ery1 {ECO:0000313|EMBL:RIV78090.1,
RC   ECO:0000313|Proteomes:UP000285092};
RA   Cheng H., Wu Y.-H., Fang C., Xu X.-W.;
RT   "Altererythrobacter sp.Ery1 and Ery12, the genome sequencing of novel
RT   strains in genus Alterythrobacter.";
RL   Submitted (AUG-2018) 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=[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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RIV78090.1}.
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DR   EMBL; QXFK01000016; RIV78090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418NHN1; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000285092; Unassembled WGS sequence.
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; cd19944; NirB_Fer2_BFD-like_2; 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   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 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; 2.
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   Reference proteome {ECO:0000313|Proteomes:UP000285092}.
FT   DOMAIN          16..294
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          332..399
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          438..485
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          499..548
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          574..638
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          647..781
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   833 AA;  90603 MW;  90DF136BF2F83B33 CRC64;
     MNAPATFDSA RPAREKLVVI GNGMAGCRAV EEILERDRER FDVVIFGAEP RVNYNRIMLS
     PVLAGEKTFD EIVLNTAEWY TENAIELIAG DPVDHIDRER KTVVSRSGRV EPYDKLLIAT
     GSDPFIIPVP GRDLPGVVTF RDLDDVDKML AAADLGGNAV VIGGGLLGLE AAHGLSLRGM
     NVTVIHLMPT LMERQLDEAA GWLLKQELER RGQTILTGAD TEEIVGKDGH VDAVRLKDGR
     EIPADIVVMA VGIRPATRLA KTGGLECERG ILVDDHMVTS DPDVVAVGEC VQHRGQCYGL
     VAPLWEMCRA LADHLTERKL DGSGGYQGSV TSTKLKVSGI DVFSAGDFSG GGEGEDIVMR
     DAARGVYKRL VLKENRIVGA VLYGDTADGN WYFDLLRKEE DISDMREGLI FGQAFALGGG
     ALADSNAAVA ALSDDAEICG CNGVSKGKVV DTILAGACSL DAVRSQCKAS ASCGSCTGLV
     ESLLALTLGD EVQAGASTMC KCTSFGHDDV RRLILEKELK AIPQVMQELH WTTPDGCASC
     RPALNYYLLC AWPGEYEDDQ KSRFVNERLH ANIQKDGTYS VVPRMWGGIT NPRELRAIAD
     VVEKFDARMV KVTGGQRLDI FGIRKEDLPA VWADLNAAGM VSGHAYGKSL RTVKTCVGSE
     WCRFGTQDST GLGVKLEQMS WGSWMPHKFK MAVSGCPRNC AEATIKDFGV VCVDSGYELH
     IGGNGGIKVR ATDLLCKVAT EEEALETCAA FIQLYREDAH YLERTAPWLE RKGLEWIKAQ
     MFDGLDAVRQ LAARFRHSQK FMQDDPWAKR AAGERRDLHS HLATVVPAGM EYA
//
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