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Database: UniProt
Entry: A0A1X1MUD4_9VIBR
LinkDB: A0A1X1MUD4_9VIBR
Original site: A0A1X1MUD4_9VIBR 
ID   A0A1X1MUD4_9VIBR        Unreviewed;       849 AA.
AC   A0A1X1MUD4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Nitrite reductase {ECO:0000313|EMBL:ORT51001.1};
GN   ORFNames=ST37_06320 {ECO:0000313|EMBL:ORT51001.1};
OS   Vibrio sp. qd031.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1603038 {ECO:0000313|EMBL:ORT51001.1, ECO:0000313|Proteomes:UP000193432};
RN   [1] {ECO:0000313|EMBL:ORT51001.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ORT51001.1, ECO:0000313|Proteomes:UP000193432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=qd031 {ECO:0000313|Proteomes:UP000193432};
RA   Chen G.;
RT   "Denovo assembling a bacteria genome.";
RL   Submitted (MAY-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   -!- 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:ORT51001.1}.
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DR   EMBL; JXQD01000018; ORT51001.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1MUD4; -.
DR   STRING; 1603038.ST37_06320; -.
DR   OrthoDB; 9768666at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000193432; 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   Reference proteome {ECO:0000313|Proteomes:UP000193432}.
FT   DOMAIN          5..303
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          320..382
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          424..471
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          560..622
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          632..771
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   849 AA;  92824 MW;  4913B6BF35E85E72 CRC64;
     MSKQRIVVVG NGMVGHKFID NLIAAERSDI DVITFSEEPR LAYDRVQLTS YFEGKTVEDL
     SLTDETYYEE NGVKFVVNEK VTQVDTNSKK VITQSGREEA YDKLVLATGS YPFVPPIPGN
     DSEHCYVYRT IEDLDAIEAG SKVSKSGVVV GGGLLGLEAA NAIKNLGLET HVVEFAPRLM
     AVQLDEGGGA LLRRKIEALG VGVHTEKATT EIVAGETSRY RMNFADGSFL ETDMIVFSAG
     IRPQDELARG GDIAIGERGG ISVDNHMLTD KEDVYAIGEC ALWDNKIFGL VAPGYQMAKV
     AAQHILEPTE ASEFTGADMS TKLKLMGVDV ASIGEVHGQT PGAQSYTYHD EIDQVYKRLI
     LSEDGSKIVG AVLVGEAESY GTLLQTKLND MPLPSNPSVL ILPNAAEDEG AAMGIEALPD
     SAQICSCFDV TKGDIKQAVA DGCTTMAALK DSTNASTGCG GCSALAKQVL DSELASLGVE
     VNNDLCEHFA YSRQELSDII RVNKIKTFDE LLTSHGTGLG CELCKPAVGS ILASFWNDYV
     LQSEHMELQD TNDIYLGNMQ KDGTYSVVPR IAGGEITPDK LIVIGEVAKE FNLYTKITGG
     QRVDLFGAQL NDLPVIWRRL VEAGFETGHA YGKSVRTVKS CVGSTWCRFG VKDSVGFAVD
     IENRYKGLRA PHKLKFAVSG CTRECAEAQC KDIGIIATEN GWNLYVCGNG GMRPRHADLF
     ATDLDDKTLI KYVDRVLMFY VRTADKLQRT SVWLENLEGG LDYLKQVVIE DKLGICDELE
     KEMAASLANY QCEWKTTIES PEKLKRFSHF INSDQRDEKL KFISVREQLI PADKVDEYAE
     NAIEVVELT
//
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