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Database: UniProt
Entry: S9TSE1_PAEAL
LinkDB: S9TSE1_PAEAL
Original site: S9TSE1_PAEAL 
ID   S9TSE1_PAEAL            Unreviewed;       801 AA.
AC   S9TSE1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Nitrite reductase [NAD(P)H], large subunit {ECO:0000313|EMBL:EPY05206.1};
GN   ORFNames=PAALTS15_21073 {ECO:0000313|EMBL:EPY05206.1};
OS   Paenibacillus alvei TS-15.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1117108 {ECO:0000313|EMBL:EPY05206.1, ECO:0000313|Proteomes:UP000015344};
RN   [1] {ECO:0000313|EMBL:EPY05206.1, ECO:0000313|Proteomes:UP000015344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TS-15 {ECO:0000313|EMBL:EPY05206.1,
RC   ECO:0000313|Proteomes:UP000015344};
RA   Strain E.A., Brown E., Allard M.W., Luo Y.L.;
RL   Submitted (MAY-2013) 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:EPY05206.1}.
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DR   EMBL; ATMT01000069; EPY05206.1; -; Genomic_DNA.
DR   RefSeq; WP_021261445.1; NZ_ATMT01000069.1.
DR   AlphaFoldDB; S9TSE1; -.
DR   PATRIC; fig|1117108.3.peg.4346; -.
DR   eggNOG; COG1251; Bacteria.
DR   UniPathway; UPA00653; -.
DR   Proteomes; UP000015344; 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; 2.
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.
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          4..280
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          316..383
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          414..463
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          480..530
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
FT   DOMAIN          555..617
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   801 AA;  88141 MW;  096CA279BC5A6B2C CRC64;
     MRKRLVMIGN GMAGARCIEE ILRRDRERYD VTMIGDEPYP NYNRIMLSPV LQGKTTFEEI
     TINDWDWYQS NNIHLLTNER VVAIDREAQE VRTDLGTVVP YDELIIATGS SAFILPVPGH
     TLEGVVGFRT IKDTKMMLEA AKQYNKAVVI GGGLLGLEAA RGLMNQGMDV HVVHLLPYLM
     EMQLDPVAAS LLRRDLEAQG MKFLMEKKTT EIYGDGRVQG LRFEDGTSVE CDLVVMAVGI
     RPNVAIAREA GLAVARGIQV NDVMQTSDPA IYAVGECAEH GGIAYGLVAP LYEQGVVLAD
     HLTDRPTEGY HGSVLSTQLK VAGCDLFSGG EIHADENTKA IVVQDEFAGA YKKVLVRDGK
     VVGVVLYGDV SDGTRLFSML KKESDIQEYT SASVLHKAGE DSGLDVASIS ANETICGCNG
     VTKGTIVGAI LENGLTTFDE VKSLTKAGGS CGKCRGMVEA ILAHTLGDKF DASAQKAAGM
     CGCTTLSRDE VVAAIREKGL QSPREVRMVL GFTHEEGCSK CRPALNYYLR MLRPETYADD
     KASRYVNERM EGNIQNDGTF SVIPRMYGGT TTPEDLIRIG EVAKKYEVPL VKITGASRIG
     LYGVKKEDVP KVWEELEMRS GYAYSKSLRN VKSCVGSRFC RFGTQDSLGL GIQLEQEIEM
     VDTPHKMKMG VTGCPRNCAE VLTKDFGVVC VENGYQLYFG GNGGTEVREC DSLTTVETEN
     EVIRFAKAYV QLYRETGIYG ERTAPWVNRM SADWVRQTLA EEAEVATLVD RFEAAKKTYS
     EAWKTALENE ERRSMYTVER P
//
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