ID K6ZNY1_9ALTE Unreviewed; 854 AA.
AC K6ZNY1;
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:GAC30598.1};
DE EC=1.7.1.4 {ECO:0000313|EMBL:GAC30598.1};
GN Name=nirB {ECO:0000313|EMBL:GAC30598.1};
GN ORFNames=GPAL_3758 {ECO:0000313|EMBL:GAC30598.1};
OS Glaciecola pallidula DSM 14239 = ACAM 615.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1121922 {ECO:0000313|EMBL:GAC30598.1, ECO:0000313|Proteomes:UP000006251};
RN [1] {ECO:0000313|EMBL:GAC30598.1, ECO:0000313|Proteomes:UP000006251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 615 {ECO:0000313|EMBL:GAC30598.1,
RC ECO:0000313|Proteomes:UP000006251};
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:GAC30598.1}.
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; BAEQ01000065; GAC30598.1; -; Genomic_DNA.
DR RefSeq; WP_006014976.1; NZ_KE386819.1.
DR AlphaFoldDB; K6ZNY1; -.
DR STRING; 1121922.GCA_000428905_03292; -.
DR OrthoDB; 9768666at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000006251; 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:GAC30598.1}.
FT DOMAIN 13..294
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 329..393
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 431..478
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 568..628
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 640..765
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 854 AA; 93428 MW; 6208A5085EF18A7A CRC64;
MVKSIISNVP KDNIVVIGNG MVGHHFVQQL RAKSPDTSIR VLSGEPRLAY DRVHLSEFFS
GKTADDLAMT TPAEYASLNV SFHTEAWVTT IDKVSKIVTI KTGQQFCYDK LVLATGSYPF
VPPIPGNQQQ HCLVYRTIED LYDIQASAQV SKIGVVVGGG LLGLEAANAL KEAGLETHVV
EFAPQLMAVQ LDTSGGRLLR DKISALGVEV HTQKATQEIV AGNSCRYRMN FADGTFLETD
MILFSAGIRP SDSLAKAHDL AMGERGGIVI DDYCLTSDKN IYAVGECALW QQRIFGLVAP
GYTMARAAVS HILNGESDKT LKFQGADMST KLKLMGVEVG SIGDAHAKTL NALSYTYENQ
PLGLYKKIVV DATQTKLLGA VLVGDTSDYD TLLQYALNAI DLPEFPESLI LPSTGDADPA
IGADALPMTA TICSCHNVSK GDIVTAIDQG SYTLSSVKSC TKASSGCGGC AALLKKVVDT
ELAKRGVEVK KDVCEHFAHS RQELFHIVKV EGITSFDVLI EQHGKGLGCE ICKPLSASIF
ASVYNDFILQ KEHLGLQDTN DIFLGNMQKD GTYSVVPRVP GGEITPEKLI LLGEVARDYH
LYTKITGGQR VDLFGARVED LPDIWERLVV GGFETGHAYA KSLRTVKSCV GSTWCRFGVQ
DSVAQAIDLE NRYKGLRAPH KIKFGVSGCT RECAEAQSKD IGIIATENGW NLYVCGNGGM
KPRHGDLFAI DLDTKTLVKY IDRILSFYIK TADRLQRTSV WMDNMEGGLG YLQDVVINDV
LGIASELEAQ MQNIVDTYQC EWKTTIENPQ LRKRFRQFVN SNQKDNNITF VQERGQIRPA
TEEEKNTINI VERV
//
