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Database: UniProt
Entry: K6XTL6_9ALTE
LinkDB: K6XTL6_9ALTE
Original site: K6XTL6_9ALTE 
ID   K6XTL6_9ALTE            Unreviewed;       866 AA.
AC   K6XTL6;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Nitrite reductase (NAD(P)H) large subunit {ECO:0000313|EMBL:GAC15026.1};
DE            EC=1.7.1.4 {ECO:0000313|EMBL:GAC15026.1};
GN   Name=nirB {ECO:0000313|EMBL:GAC15026.1};
GN   ORFNames=GLIP_2400 {ECO:0000313|EMBL:GAC15026.1};
OS   Aliiglaciecola lipolytica E3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Aliiglaciecola.
OX   NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC15026.1, ECO:0000313|Proteomes:UP000006334};
RN   [1] {ECO:0000313|EMBL:GAC15026.1, ECO:0000313|Proteomes:UP000006334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3 {ECO:0000313|EMBL:GAC15026.1,
RC   ECO:0000313|Proteomes:UP000006334};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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:GAC15026.1}.
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DR   EMBL; BAEN01000046; GAC15026.1; -; Genomic_DNA.
DR   RefSeq; WP_008844831.1; NZ_BAEN01000046.1.
DR   AlphaFoldDB; K6XTL6; -.
DR   STRING; 1127673.GLIP_2400; -.
DR   eggNOG; COG1251; Bacteria.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000006334; 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:GAC15026.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006334}.
FT   DOMAIN          9..296
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          327..392
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          429..473
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          566..628
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          638..763
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   866 AA;  94614 MW;  158FA2E29BDEDF86 CRC64;
     MTTNEHLTRI VIVGNGMVGH HFVEQLIQQS NEVYGKNQFH ITVLSAEPRL AYDRVHLSEY
     FSGKTADELS LTSAEHYQEL GVDFQVNARV DQIDKQAKMV TIESGAVFEY DKLILATGSF
     PFVPPIPGND QPHCLVYRTI EDLEAISASA KVSKVGVVVG GGLLGLEAAN ALKEAGLKTH
     VVEFAPQLMA VQVDVSGGRV LKDKIEELGV EVHTQKATQS IEAGENSRYK MVFADGEILE
     TDMILFSAGI RPQDKLAREF GIVIGERGGI VVNDHCLTSD PDIYAIGECA LWNNFIFGLV
     APGYTMARAA ASNIVGGDVV FEGADMSTKL KLMGVEVGSI GDAHAREHGA QTYTYEDQVA
     GVYKKIVINA ETNKLTGAVL VGDTGDYDTL LQYALNEIDL PEFPESLILP SFGDAAPTLG
     ADALPETAMI CSCHNVTKGD IIASLDGGAC DLAEIKSCTK ASTGCGGCAA LLKSVTDSEL
     EKRGVEVKKD ICEHFAYSRQ ELYHMVQIGQ IKTFDELLSK HGSGIGCEVC KPAAASILAS
     IWNDFVLEKP HVTLQDTNDT YLANMQKNGT YSVVPRIAGG EITPDKLIVL GQVAKKYNLY
     TKVTGGQRID LFGARVEQLP LIWEELIEAG FETGHAYAKS LRTVKSCVGS TWCRYGVQDS
     VGQAIDLENR YKGLRSPHKL KFAVSGCTRE CAEAQSKDIG VIATENGWNL YVCGNGGMKP
     RHADLFATDL DTETLVKYID RVLMFYVRTA DRLQRTSVWM ENMEGGLDYL KDVVINDSLG
     LGAELEQQMQ HVVDTYQCEW KTAVTSEQSR KRFRQFVNSE KSDANIIFVE ERDQIRPATE
     IEIDQILGVK KPVKAAATSI NIVEVE
//
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