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Database: UniProt
Entry: A0A1Y5T347_9RHOB
LinkDB: A0A1Y5T347_9RHOB
Original site: A0A1Y5T347_9RHOB 
ID   A0A1Y5T347_9RHOB        Unreviewed;       814 AA.
AC   A0A1Y5T347;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Nitrite reductase [NAD(P)H] {ECO:0000313|EMBL:SLN51237.1};
DE            EC=1.7.1.4 {ECO:0000313|EMBL:SLN51237.1};
GN   Name=nasD_2 {ECO:0000313|EMBL:SLN51237.1};
GN   ORFNames=AQS8620_02197 {ECO:0000313|EMBL:SLN51237.1};
OS   Aquimixticola soesokkakensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Aquimixticola.
OX   NCBI_TaxID=1519096 {ECO:0000313|EMBL:SLN51237.1, ECO:0000313|Proteomes:UP000193862};
RN   [1] {ECO:0000313|EMBL:SLN51237.1, ECO:0000313|Proteomes:UP000193862}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8620 {ECO:0000313|EMBL:SLN51237.1,
RC   ECO:0000313|Proteomes:UP000193862};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (MAR-2017) 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}.
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DR   EMBL; FWFS01000008; SLN51237.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y5T347; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000193862; 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; 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; 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; 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   ECO:0000313|EMBL:SLN51237.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193862}.
FT   DOMAIN          5..285
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          317..383
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          420..467
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          482..532
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          557..620
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          630..769
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   814 AA;  87810 MW;  1C54519570F0BD3D CRC64;
     MSKQNLVIVG NGMAPGRLLE HLFEATDSYN VTIFNAEPRV NYDRIMLSPV LSGEKSFEDI
     VIHSEEWYAG HGITLHKGAK VSKIDRAAKT VTSENGITAP YDKLVIATGS SPFIIPVPGK
     DLDGVLAYRD LEDTYGMMKA AKAGGRAVVI GGGLLGLEAA AGLRMQGMEV TVIHLMASLM
     ERQLDPAAGF LLQRELEGRG IEVLCEANTK QILGTDKVEG VELADGRIID ASLVVMAVGI
     RPSVQLAKDA GLEVNRGIVT GFDLKTSDPD IYSVGECVEV GGMVYGLVAP LYQMAKVAAA
     HLSGPSDAAF QHVETPTKLK VTGVNLYSVG DFAEGPDRED IVLRNASAGT YKRVILRDNK
     VIGAVMYGDV ADGGWYNEML KSGEDVSDKH ETLIYGQMFQ GGGAVDPLAI VAGLSDDAEI
     CGCNGICKGQ ITSAITEKGL TSLAEVRAHT KASASCGTCT GLVQDLMTIT LGEDAAAVPE
     GMCGCTHLGH GDVRRLIVAK ELKSIPAVMQ ELEWTTPEGC AKCRPALNYY LISDWPGEYA
     DDMQSRFINE RVHANIQKDG TYSVVPRMWG GITTPDELRA IADVADKFDI PTVKVTGGQR
     IDLLGVKKED LLPVWKDLND AGMISGAAYA KGLRTVKTCV GKDWCRFGTQ DSTGLGVKLE
     QFLWGSWAPA KLKLAVSGCP RNCAESTCKD IGIVCVDSGY EVLYGGAAGL HIQGTTKLGN
     VATEQDVIEV VGALTQFYRE TGYYLERIYK WADRIGYDHV KAMVFDDLEQ RHAYYERFVY
     SQKFAQIDPW AERVAGAEAH EFSPMAEIKL EAAE
//
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