ID A0A1Z4ECE7_9MYCO Unreviewed; 720 AA.
AC A0A1Z4ECE7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Nitrite reductase large subunit {ECO:0000313|EMBL:BAX90619.1};
GN Name=nirB_1 {ECO:0000313|EMBL:BAX90619.1};
GN ORFNames=MSG_00454 {ECO:0000313|EMBL:BAX90619.1};
OS Mycobacterium shigaense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=722731 {ECO:0000313|EMBL:BAX90619.1, ECO:0000313|Proteomes:UP000217736};
RN [1] {ECO:0000313|Proteomes:UP000217736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UN-152 {ECO:0000313|Proteomes:UP000217736};
RA Fukano H., Yoshida M., Kazumi Y., Ogura Y., Mitarai S., Hayashi T.,
RA Hoshino Y.;
RT "Complete Genome Sequence of Mycobacterium shigaense.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; AP018164; BAX90619.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4ECE7; -.
DR KEGG; mshg:MSG_00454; -.
DR Proteomes; UP000217736; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:InterPro.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
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 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; 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; PF03460; NIR_SIR_ferr; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF18267; Rubredoxin_C; 1.
DR PRINTS; PR00368; FADPNR.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 2..290
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 324..384
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 426..473
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 558..605
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT REGION 681..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..702
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 74965 MW; 6D77BF17610E9DF1 CRC64;
MVVVGHGMVG HRLVEALRAR DDDGTWQITV LAEESDAAYD RVGLTSYTES WDRALLALPG
NDYAGDERVR LLLNARVTEI DRAAKSVLTA DGQRHDYDTL VLATGSHAFV PPVPGHDLPG
CHVYRTLDDL DAIRAAAEQA HHAGHDSAGV VIGGGLLGLE AANALRQFGL QTHVVEMMPR
LMAQQIDEGG GALLARMITD LGIAVHVGTG TESIEAVGRP DGSSSMRVRL TDGEVVDAGV
VIFAAGIRPR DELAAAAGLK LAERGGVFTD LACQTSDPDI YAVGEVAAID GRCYGLVAPG
YTSAEVVVDR LLGGGAEFPE ADMSTKLKLL GVDVASFGDA MGATANCLEV AINDAVNRTY
AKLVLSDDAK TLLGGVLVGD ASAYGVLRPM VGSELPGDPL ALIAPAQSGG GASALGVGAL
PDSAQICSCN NVTKGDLKCA IADGCADVPA LKSCTAAGTS CGSCVPLLKQ LLEAEGVEQS
KALCEHFSQS RAELFEIISA TELRTFSGLL QRYGRGRGCD ICKPVVASIL ASTGSEHILD
GEQAALQDSN DHFLANIQKN GSYSIVPRVP GGDIKPEHLI LIGQIAQDFG LYTKITGGQR
IDMFGARVDQ PSGDLAATGG RRHGVGPRLR QGAAHGEKLC GQRLVPVRAA GFGPAGHRPG
AALPRSAGAA QDQAGCLGMC AGMRRGPRQG RRHHRHRKGL ESLRSRQRRD DSAACPAAGR
//
