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Database: UniProt
Entry: I2HMB6_9BACI
LinkDB: I2HMB6_9BACI
Original site: I2HMB6_9BACI 
ID   I2HMB6_9BACI            Unreviewed;       805 AA.
AC   I2HMB6;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Assimilatory nitrite reductase subunit {ECO:0000313|EMBL:EIF11875.1};
GN   ORFNames=MY7_0162 {ECO:0000313|EMBL:EIF11875.1};
OS   Bacillus sp. 5B6.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1127743 {ECO:0000313|EMBL:EIF11875.1, ECO:0000313|Proteomes:UP000005799};
RN   [1] {ECO:0000313|EMBL:EIF11875.1, ECO:0000313|Proteomes:UP000005799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5B6 {ECO:0000313|EMBL:EIF11875.1,
RC   ECO:0000313|Proteomes:UP000005799};
RX   PubMed=22740678; DOI=10.1128/JB.00682-12;
RA   Kim B.K., Chung J.H., Kim S.Y., Jeong H., Kang S.G., Kwon S.K., Lee C.H.,
RA   Song J.Y., Yu D.S., Ryu C.M., Kim J.F.;
RT   "Genome Sequence of the Leaf-Colonizing Bacterium Bacillus sp. Strain 5B6,
RT   Isolated from a Cherry Tree.";
RL   J. Bacteriol. 194:3758-3759(2012).
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:EIF11875.1}.
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DR   EMBL; AJST01000001; EIF11875.1; -; Genomic_DNA.
DR   RefSeq; WP_007609279.1; NZ_AJST01000001.1.
DR   AlphaFoldDB; I2HMB6; -.
DR   PATRIC; fig|1127743.3.peg.154; -.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000005799; 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   Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 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; 2.
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.
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..281
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          317..384
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          416..465
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          481..530
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          556..618
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          626..764
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   805 AA;  88446 MW;  13E3945A9E720133 CRC64;
     MGKKQLVLVG NGMAGVRAIE EILRVSKDEF EITIFGAEPH PNYNRILLSK VLQGDTDIQD
     ITLNDWNWYK ENNIQLYTGE TVIKVDTENK TIITDADRIQ PYDELILATG SVPFILPIPG
     ADKQGVTAFR DIKDTDTMLA ASKQYKKAAV IGGGLLGLEA ARGLLNLGMD VSVIHLAPFL
     MERQLDAAAG RLLQNELEKQ GMTFFLEKQT EEILGTDRVE GVRFKDGTSI EADLVVMAVG
     IRPNTQLGTE SGIPVNRGII VNDYMQTDIP HIYAVGECAE HRGIAYGLVA PLYEQAKVLA
     KHICGIDTKP YEGSVLSTQL KVSGVEVFSA GDFNESEDKK AIKVFDEQDG IYKKIVLRGN
     QIVGAVLFGD SSEGGRLFSM IQKEADISET SKISILQPLD QEAGASMTAA MSDDEIICGC
     NGVSKGAIIQ AIQEKGCTST DEIKACTGAS RSCGGCKPLV EDILQYTLGS EFDASAQKEA
     ICGCTSLSRD EVVEEIKAKG LSHTREIMNV LGWKTPEGCS KCRPALNYYL GMINPATYED
     DRTSRFVNER MHANIQKDGT YSVVPRMYGG VTNSQDLRKI ADVVDKYEIP LVKMTGGQRI
     DLIGVKKEDL PKVWAELDMP SGYAYGKTLR TVKTCVGEQF CRFGTQDSMA LGIALEKKFE
     GLNTPHKVKM AVSACPRNCA ESGIKDLGVV GIDGGWELYV GGNGGTHLRA GDLLMKVKTN
     EEVLEYAGAY LQYYRETANY LERTSAWLER VGLSHVQSVL NDPEKRQELN DRMNETLSVH
     KDPWQYFLKD KKASKDLFEN VVTTS
//
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