ID A0A1Y5RI94_9RHOB Unreviewed; 817 AA.
AC A0A1Y5RI94;
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:SLN15311.1};
DE EC=1.7.1.4 {ECO:0000313|EMBL:SLN15311.1};
GN Name=nasD {ECO:0000313|EMBL:SLN15311.1};
GN ORFNames=PSA7680_00392 {ECO:0000313|EMBL:SLN15311.1};
OS Pseudoruegeria aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoruegeria.
OX NCBI_TaxID=393663 {ECO:0000313|EMBL:SLN15311.1, ECO:0000313|Proteomes:UP000193409};
RN [1] {ECO:0000313|EMBL:SLN15311.1, ECO:0000313|Proteomes:UP000193409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7680 {ECO:0000313|EMBL:SLN15311.1,
RC ECO:0000313|Proteomes:UP000193409};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWFQ01000002; SLN15311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5RI94; -.
DR OrthoDB; 9768666at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000193409; 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; 1.
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:SLN15311.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193409}.
FT DOMAIN 5..281
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 318..385
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 422..468
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 484..533
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 559..622
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 633..772
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 817 AA; 88495 MW; EF4A3077E97841BF CRC64;
MPKQNLVIIG AGMASGRALE DLLALAPDAY DVTLFNAEPR GNYNRIMLSP VLSGEKCYED
IVIHTAEWYE ENGVTCRFGE KIAKVDRARK VVVSETGEEV PYDKLIFGTG SNPFIIPLPG
HDLEGVIAYR DLEDTNTMIA LGEKPGAKAV VIGGGLLGLE AAAGLALRGV DVTVVHIMGH
LMERQLDEAA GYLLRKALVD KGIKVMCSAN SKEILGENGR VKALRLEDGT ELPCDLLVMA
VGIRPNIALA QEAGLATGRG IHVDDQMVTS DPDIYAVGEC VEHDGAVFGL VAPLYDQARV
LAKTLVGEEA KFVQKELSTK LKVTGCDLFS AGDFAEGEGR EDIVLRDPAR GVYRRLVIEN
DRIVGAVMYG DTADSNWFFG LIKDGTDISE MRDTLIFGPA YQGGEPLDPM AAVAALPDDA
EICGCNGVCK GDIVAAIQAG AHDLGAVRAT TKASASCGTC TGLVEQVLGA TLGDDFVIPA
AQGMCGCTDL SHEDVRRMIK SQELKSQQAV WQACGWKTVN GCHVCRPAVN YYLLADWPLD
YQDDPQSRFV NERNHANIQK DGTYSVVPRM WGGITTPAEL RAIADAAEKY NVPTVKVTGG
QRIDLLGVKK EDLPAMWYDL NQAGLVSGHA YSKGLRTVKT CVGKEHCRFG TQDSTGLGIK
LEKLLWGSWT PHKVKLGVSG CPRNCAEATC KDVGIVCVDS GFEVSVAGAA GMDVKETELL
AKVATEEEAI ALTTAFIQLY RENAKYLDRG YKWVAKVGLD WVKEQIVEDL ENRTALVERF
EISQSIYRKD PWAEQATPDY REKKWNPIAD LTLEAAE
//
