ID A0A2A3XYF6_9MICC Unreviewed; 869 AA.
AC A0A2A3XYF6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=CIK76_10870 {ECO:0000313|EMBL:PCC28709.1};
OS Glutamicibacter sp. BW80.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Glutamicibacter.
OX NCBI_TaxID=2024404 {ECO:0000313|EMBL:PCC28709.1, ECO:0000313|Proteomes:UP000218725};
RN [1] {ECO:0000313|EMBL:PCC28709.1, ECO:0000313|Proteomes:UP000218725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BW80 {ECO:0000313|EMBL:PCC28709.1,
RC ECO:0000313|Proteomes:UP000218725};
RX PubMed=28644126;
RA Bonham K.S., Wolfe B.E., Dutton R.J.;
RT "Extensive horizontal gene transfer in cheese-associated bacteria.";
RL Elife 6:e22144-e22144(2017).
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide, a step in the
CC biosynthesis of sulfur-containing amino acids and cofactors.
CC {ECO:0000256|ARBA:ARBA00003247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] =
CC 7 H(+) + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite;
CC Xref=Rhea:RHEA:23132, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.8.7.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000993};
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:PCC28709.1}.
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DR EMBL; NRGV01000032; PCC28709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3XYF6; -.
DR UniPathway; UPA00653; -.
DR Proteomes; UP000218725; 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:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd19944; NirB_Fer2_BFD-like_2; 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; 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 Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 9..307
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 340..406
FT /note="NADH-rubredoxin oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18267"
FT DOMAIN 437..492
FT /note="BFD-like [2Fe-2S]-binding"
FT /evidence="ECO:0000259|Pfam:PF04324"
FT DOMAIN 581..642
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 653..791
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
SQ SEQUENCE 869 AA; 91793 MW; 9397B36CC6251EDA CRC64;
MGTAHGSRRI VVVGGGPAAH RFTQAISNRE PSDLHITVLT EETHIPYDRV ALSQALTNPG
VDLTLGEVEL WERAHVTLET GAAVTELDSI KQTVRTADGR SFEYDQLVLA TGSNAATLPI
PGAEHTHVYR TLEDVWAIAE QVRELTESLG RAPVVATIGG GLLGLEAAAG AQALGAEAVV
IDGGKWLMGT QLDEGAGQAM GRLIADTGFT VHGGVFPKEI LASAETGLVC GVLMADERTI
DADMVIVSIG VRPRDEIARN YNAALDASES SQPRFGIGPR GGIEIDAGCA TAIPNVYAIG
EVANFEGLCI GLVAPANAMA EVVAERLQGG TAEFAGFDTA TKLKLSGVDV ASFGDGFART
EGALEVVYAD APRGLYQKVV VSSDAKVLLG GIFVGDATPY QSLRPLLGRE LPGEPGAYLS
ALGGEAPQGE LPDEAVLCSC NNVSAGSIRD AVGGCGSCEG SEPVTKLSEL KGCTRAGTQC
GSCVPMLKKL MEAEMLKNGA EVSAAMCEHF ELSRAQLFEA VRLAGLTSYP QIMERFGKGA
GCDICKPVIA SVLASQTSGH PMEAGLAGAQ DTNDRVMANM QKDGTYSVVP RIPGGEITPE
KLGVIAAVAA KYNLYTKLTG GLRIDMFGAR LEQLPEIWKE LVDAGFESGQ AYGKSLRNVK
TCVGSSWCRY GMLDSVAMGI EMELRYRGLR APHKFKMGVS GCARECAEAR AKDVGVIATA
EGWNLYVGGN GGANPAHAQL LAGGLDDATL LRYIDRYLMY YIRTADRLQR TAHWMQDLDG
GIEHVKAVVV EDSLGLGAEL EAAMETHVGN YQDEWAATLA DPEKLRRFRS FVNAPDQKDE
ELSYIPERGQ HRPAEPVRLG ATIGIGAPS
//
