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Database: UniProt
Entry: A0A099L942_9GAMM
LinkDB: A0A099L942_9GAMM
Original site: A0A099L942_9GAMM 
ID   A0A099L942_9GAMM        Unreviewed;       856 AA.
AC   A0A099L942;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Nitrite reductase (NAD(P)H) {ECO:0000313|EMBL:KGJ99376.1};
DE            EC=1.7.1.4 {ECO:0000313|EMBL:KGJ99376.1};
GN   ORFNames=ND16A_3897 {ECO:0000313|EMBL:KGJ99376.1};
OS   Thalassotalea sp. ND16A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Thalassotalea.
OX   NCBI_TaxID=1535422 {ECO:0000313|EMBL:KGJ99376.1, ECO:0000313|Proteomes:UP000029848};
RN   [1] {ECO:0000313|EMBL:KGJ99376.1, ECO:0000313|Proteomes:UP000029848}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND16A {ECO:0000313|EMBL:KGJ99376.1,
RC   ECO:0000313|Proteomes:UP000029848};
RA   Stelling S.C., Techtmann S.M., Utturkar S.M., Alshibli N., Brown S.D.,
RA   Hazen T.C.;
RT   "Draft Genome Sequence of Thalassotalea sp. strain ND16A Isolated from
RT   Eastern Mediterranean Deep Water.";
RL   Submitted (AUG-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=[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:KGJ99376.1}.
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DR   EMBL; JQDZ01000031; KGJ99376.1; -; Genomic_DNA.
DR   RefSeq; WP_033076741.1; NZ_JQDZ01000031.1.
DR   AlphaFoldDB; A0A099L942; -.
DR   STRING; 1535422.ND16A_3897; -.
DR   PATRIC; fig|1535422.3.peg.1132; -.
DR   eggNOG; COG1251; Bacteria.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000029848; 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   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:KGJ99376.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029848}.
FT   DOMAIN          12..298
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          323..388
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          424..468
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          561..622
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          633..769
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   856 AA;  93400 MW;  C9DABA89EEFE48D6 CRC64;
     MSTSDLSQSK QNIVVVGNGM VGHHFVEQLS QFDGYNITVL SAESRLAYDR VHLSEYFSGK
     TADDLALTTP ENYQQLGVNF ELDAKVTQID KAAKTVTTES GDTFSYDKLV LATGSYAFVP
     PIPGKDREHC LVYRTIDDLD AIQASANTGK VGVVVGGGLL GLEAANALKE LGLDTHVVEF
     APQLMGVQLD QAGGLLLKNK IESLGVTVHT EKATNVIVDG DDCVHKMEFA DGSHLETDLI
     LFSAGIRPYD NLAREFDLTL GERGGIVVNN QCQTSDDDIY AIGECALWNN FIYGLVAPGY
     SMAKVAASHI IGGEDKFTGA DMSTKLKLMG VEVGSIGDAH AKTAGAQCYT YQNDRDNVYK
     KMVVSQDGKT LLGAVLVGDT SEYDALLQYA LNGIELPENP DALILPSSGE KPTLGVDSLP
     DTATICSCLN VTKGDIIAAV DAGATDVGTI KSDTKATTGC GGCAALLKTV ADNEFAKRGL
     EVKKDICSHF VYSRTELFHI VKAEKIKTFD ELVSKHGKGM GCEICKPAVA SILASVYNDY
     ILEDDHLHLQ DTNDTYLGNM QKDGTYSVVP RMPGGEVTPD KLIVIGEVAK EYNLYTKVTG
     GQRIDLFGAR VEQLPAIWKR LIDAGMETGH AYGKSLRTVK SCVGSTWCRY GVQDSMSMAI
     FLEERYKGLR SPHKIKFAVS GCTRECAEAQ SKDIGVIATE NGWNLYVSGN GGMKPRHGDL
     FATDLDDATL IKYIDRYLMF YVRTADRLQR TSVWLENLEG GLEYMQKVVK DDHLGINDEL
     ENQMDAVVAT YQCEWKTTVD SPEKLKRFRQ FVNSDKQDVN IQFVDEREQI RPATLTEKAE
     QGLLIDTVNI TEVEPA
//
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