ID A0A1B1EL29_VIBNA Unreviewed; 846 AA.
AC A0A1B1EL29;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Nitrite reductase large subunit {ECO:0000313|EMBL:ANQ29461.1};
GN ORFNames=BA894_24155 {ECO:0000313|EMBL:ANQ29461.1};
OS Vibrio natriegens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=691 {ECO:0000313|EMBL:ANQ29461.1, ECO:0000313|Proteomes:UP000092577};
RN [1] {ECO:0000313|EMBL:ANQ29461.1, ECO:0000313|Proteomes:UP000092577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 16374 {ECO:0000313|EMBL:ANQ29461.1,
RC ECO:0000313|Proteomes:UP000092577};
RA Weinstock M.T., Hesek E.D., Wilson C.M., Gibson D.G.;
RT "Developing Vibrio natriegens as a novel, fast-growing host for
RT biotechnology.";
RL Submitted (JUL-2016) 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; CP016352; ANQ29461.1; -; Genomic_DNA.
DR RefSeq; WP_065298790.1; NZ_CP016352.1.
DR AlphaFoldDB; A0A1B1EL29; -.
DR STRING; 691.BA893_20495; -.
DR OrthoDB; 9768666at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000092577; Chromosome 2.
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}.
FT DOMAIN 5..301
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 320..381
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 423..471
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 560..621
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 632..768
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 846 AA; 93351 MW; B7DC4036C1F4FA65 CRC64;
MSKQKIIVVG NGMVGHKFID TLIQSEQNNI EVVTFSEEPR LAYDRVQLTS YFTGKTVDDL
SLTSEGYYQS NGIKYLLNEK VSQVNPDDKQ IVTSSGRVEN YDKLVLATGS YPFVPPIPGN
EKEFCHVYRT IEDLDEIERS SKESKVGVVI GGGLLGLEAA NAIKNLGLET HVVEFAPRLM
AVQLDQDGGD LLRRKIEALG VTVHTEKATT EIIDGNECRY RMNFSDGTHI DTDMIVFSAG
IRPQDELARN SSIEIGERGG IMINNHCQTN YEDIYAIGEC ALWEQRIFGL VAPGYQMAKV
AAQHILSTDE AAQFTGADMS TKLKLMGVDV ASIGDVHGQT AGALSYTYKD EIEQVYKRLI
VSEDKKKIVG AVLVGDATAY GNLLQIRQND LPLPENPSVL ILPNVAEDES AGLGIDALPD
SAVICSCFDV TKGSIKQAVA AGCTTMAALK ETTNASTGCG GCSALAKQVL DSELEKLGVE
VNNHVCEHFA YSRQELSDLI RVNKIKTFDE LLEQYGQGLG CEVCKPTAGS ILASYWNDYI
LHDDHIELQD TNDIYLGNMQ KDGTYSVVPR VAGGEITPEK LIVIGEVARD FDLYTKVTGG
QRIDLFGAQL NDLPLIWKRL VDAGFETGHA YGKSVRTVKS CVGSTWCRYG VGNSVGFAID
LENRYKGLRS PHKLKFAVSG CTRECAEAQS KDIGVIATDK GWNLYVCGNG GMRPRHADLL
ATDLDDETLI KYVDRVLMFY IRTADRLQRT SVWLENLEGG IDYLKEVVID DKLGLADELE
KSMQDSLANY QCEWKTTLES PEKLRRFSHF INSPDRDESL QFVTIREQKF PKKTADELAI
EVVEVS
//
