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Database: UniProt
Entry: A0A3N4MCG9_9BACT
LinkDB: A0A3N4MCG9_9BACT
Original site: A0A3N4MCG9_9BACT 
ID   A0A3N4MCG9_9BACT        Unreviewed;       838 AA.
AC   A0A3N4MCG9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Nitrite reductase large subunit {ECO:0000313|EMBL:RPD41391.1};
GN   ORFNames=EG028_08715 {ECO:0000313|EMBL:RPD41391.1};
OS   Chitinophaga barathri.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1647451 {ECO:0000313|EMBL:RPD41391.1, ECO:0000313|Proteomes:UP000279089};
RN   [1] {ECO:0000313|Proteomes:UP000279089}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLT18 {ECO:0000313|Proteomes:UP000279089};
RA   Zong Y.;
RT   "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL   Submitted (NOV-2018) 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:RPD41391.1}.
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DR   EMBL; RMBX01000004; RPD41391.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4MCG9; -.
DR   OrthoDB; 9792592at2; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000279089; 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:UP000279089}.
FT   DOMAIN          1..299
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          322..391
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          425..473
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          562..624
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          634..770
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   838 AA;  90896 MW;  C7DFB5E29EABF735 CRC64;
     MKIVVIGNGM VGHKFCEKIT QKLGTNTARI VIFGEETLPA YDRVHLSEYF AGKTAEDLSL
     APVDWYASQG ITLYLGDPVH IIDRQQKTVT SLKGITETYD FLVMATGSAA FVPNIAGTDK
     KGVFIYRTIE DLELMKSYAP RASRGTVIGG GLLGLEAAKA LLDLGISRTS VIEFAPRLMP
     RQIDDKGSFV LQHKLQSLGL QVLTGKNTSA ILGEETITGL AFSDGTSLDT DMLVISAGIK
     PRDELAAACG LETGPRGGIV VNDLLQSSDP SIYAVGECAL YNGMIYGLVA PGYEMAEVAA
     THIIASYTEK EPVKSFTGFD MSTKLKLIGV DVASFGNPFT PPDQSHSIVM EDSVSGVYQR
     INVSQDGKYL LGGILIGNAD AYNMLLQTCK NNIPLPANPA DVLLGPRNGG APSGAGVDAL
     PDEAVICSCE SISKAAICQA VEAGHETLDA VKKCTKAGTC CGGCTPMVKD LITATMKAQG
     KYIRNVVCEH FDYSRQELLD LIKVKSLRSF DEALDHYGHG EGCEVCKPVI SSILASLWND
     MILAKGNDTA QDSNDRYLAN IQKGGTYSIV PRIPGGEITP EKLIVIGTIA KEYNLYTKIT
     GGQRIDMFGA HLGDLPAIWE ALIAAGFESG HAYGKALRTV KSCVGSTWCR FGLHDSVSYA
     IRIEERYRGL RAPHKIKSAV SGCIRECAEA QSKDFGIIAT EKGWNLYVCG NGGSKPQHAL
     LLAQDLDSET CIRYIDRFLM FYIKTADPLT RTATWLNKLE GGIDYLRNVV VNDSLGIAES
     LETEMQSLVD SYKCEWKEVV ESPELRKKFS HFINAPEEKD PTVKFETLRE QKKAADWK
//
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