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Database: UniProt
Entry: A0A1T4KYW0_VIBCI
LinkDB: A0A1T4KYW0_VIBCI
Original site: A0A1T4KYW0_VIBCI 
ID   A0A1T4KYW0_VIBCI        Unreviewed;       829 AA.
AC   A0A1T4KYW0;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Assimilatory nitrite reductase (NAD(P)H) large subunit {ECO:0000313|EMBL:SJZ47655.1};
GN   ORFNames=SAMN02745782_00390 {ECO:0000313|EMBL:SJZ47655.1};
OS   Vibrio cincinnatiensis DSM 19608.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1123491 {ECO:0000313|EMBL:SJZ47655.1, ECO:0000313|Proteomes:UP000190834};
RN   [1] {ECO:0000313|EMBL:SJZ47655.1, ECO:0000313|Proteomes:UP000190834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19608 {ECO:0000313|EMBL:SJZ47655.1,
RC   ECO:0000313|Proteomes:UP000190834};
RA   Peterson S.W.;
RL   Submitted (FEB-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; FUXB01000002; SJZ47655.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4KYW0; -.
DR   STRING; 1123491.SAMN02745782_00390; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000190834; 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   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}.
FT   DOMAIN          4..287
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          318..384
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          414..462
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          551..611
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          623..748
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   829 AA;  90984 MW;  2D7CB2E902387E13 CRC64;
     MMEQIVIVGN GMVGHHLVAQ LVEKQAHLEK RITVIGEERF IAYDRVQLSS LFSGKSHDDL
     MLSSEEWYRK QGINLILGCQ VTEINRAQKK LILDEDEVLG YDRLILATGS YPFVPPVPGR
     ERDNIFVYRT LEDLSAIRLA CQGAKSGAVI GGGLLGLEAA NALRLLGLET HVVEFAPRLM
     PVQLDDGGGA LLKSKIEHLG LKVHTSTVTE KIIDGESAKH RMVFKDAPAL EVDVIVFSAG
     IRPQDTLARQ AGLEIGERGG IVISDQCLTS DKHIYAIGEC ALWQQKIFGL VAPGYAMARV
     VADHLLGKSH AFSGADMSTK LKLLGVDVAS IGDAQMQSEG AKELVLQDTN QGTYKKLVVD
     ESATRLLGAI LVGDSSDYDA LLQAYLNQTR LPEHPAHLLF DSSLLRGEMA DSSVICSCHN
     VTKGALVAAI HAGATELAEL KAVTKAGTGC GGCSGMVKSV LDAELVTMGM EVNHHLCEHF
     AYSRQELFHL CQVEQIKDFA TLLDKHGQGL GCDICKPTAA SVFASLWNEH IMQPDLSALQ
     DSNDAFMANL QKDGSYSVVP RVAGGEITPD KLIVLGEVAK RYDLYTKITG GQRVDLFGAQ
     MEQLPEIWQT LINAGFETGH AYGKSLRTVK SCVGSTWCRY GVDDSVGLAI ELEHRYKGLR
     APHKLKFAVS GCTRECAEAQ SKDIGVIATE KGWNLYVCGN GGMRPRHGDL FAVDLSKDEL
     VVLIDRVLMF YVRTADRLQR TSVWLDNLEG GVRYLKQVII EDSLGVCEQL EAQMQHVVDT
     YQCEWKSTLE SEQKLRKFRP FINHQQGSMA LNYQRLREQR IPAEQGEIS
//
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