ID A0A1C2GR16_9SPHI Unreviewed; 832 AA.
AC A0A1C2GR16;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Nitrite reductase large subunit {ECO:0000313|EMBL:OCX53901.1};
GN ORFNames=BEL04_06355 {ECO:0000313|EMBL:OCX53901.1};
OS Mucilaginibacter sp. PPCGB 2223.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1886027 {ECO:0000313|EMBL:OCX53901.1, ECO:0000313|Proteomes:UP000095113};
RN [1] {ECO:0000313|EMBL:OCX53901.1, ECO:0000313|Proteomes:UP000095113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PPCGB 2223 {ECO:0000313|EMBL:OCX53901.1,
RC ECO:0000313|Proteomes:UP000095113};
RA Seilhamer J.J.;
RL Submitted (AUG-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}.
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:OCX53901.1}.
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; MDJS01000001; OCX53901.1; -; Genomic_DNA.
DR RefSeq; WP_066001415.1; NZ_MDJS01000001.1.
DR AlphaFoldDB; A0A1C2GR16; -.
DR STRING; 1886027.BEL04_06355; -.
DR OrthoDB; 9792592at2; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000095113; 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; cd19943; NirB_Fer2_BFD-like_1; 1.
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:UP000095113}.
FT DOMAIN 5..284
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 317..387
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 421..469
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 557..619
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 629..754
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 832 AA; 91053 MW; 740A93C7D3E2BB24 CRC64;
MSKPTVIVVG NGMVGYKFCE KLVSRSADFK IIVFGEEPRR AYDRVHLSEY FSGRSAEDLS
MSSSSWYAEN GIELLLGDPV QEIDRAHKTV HSSKGITLKY DYLVLATGSS AFVPDIPGVE
KAGVFVYRTI EDLELIKAYA ANAKVGAVMG GGLLGLEAAK AVLDLGIPEA HVIEFAPRLM
PRQIDSMGSA MLQSKLKSLG LNIHLNKSTQ CITGDHQISG LKFNDESVLP VDMLVISAGI
RPRDELAKLA GLQIGTRGGI LVNSKMQTSD ESIFAIGECA LFDGMIYGLV APGYEMADVV
VSHLAEVNKE FNGFDMSTKL KLIGVDVASF GDAFITEPDC RTIIFEDTHK GVYKRINIST
DGKYLLGGIL IGDAEAYNML LQTVNNKLVL PPSPEDLLLG ARGGDSADAG AGVMGLPDDA
LICSCEAVTK GAICNAVCEH DITTVDAMKK CTKAGTGCGG CVPMVKDLIV GTMKANGQYI
KNVICEHFDH SRQELLDLIR INNIKHYDEV LDHYGRGDGC EVCKPVVASI LSGLWNDLIV
KQAPIQDSND RYLANIQKGG TYSVVPRIPG GEITPDKLIV IGRVAKKYNL YTKITGGQRI
DLFGAHVSDL PQIWEELIEA GFESGHAYGK SLRTVKSCVG STWCRFGLHD SVTFAIEVEN
RYKGIRSPHK LKGGVSGCIR ECAEAQAKDF GIIATEKGWN LYVCGNGGSK PQHAQLLAAD
IDKETCIKYL DRFLMFYIKT ADPLTRTATW LNKMDGGMSY LKNVIINDSL GIGEQLEEDI
QALIDTYHCE WKEVVENPEL RKRFNHFVNA PDEKDPHVQF EPMREQVRAR EW
//
