ID F2RAY6_STRVP Unreviewed; 565 AA.
AC F2RAY6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN OrderedLocusNames=SVEN_5919 {ECO:0000313|EMBL:CCA59205.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA59205.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA59205.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
RN [2] {ECO:0000313|EMBL:CCA59205.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 10712 {ECO:0000313|EMBL:CCA59205.1};
RA Bibb M.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; FR845719; CCA59205.1; -; Genomic_DNA.
DR RefSeq; WP_015037100.1; NZ_JABVZO010000037.1.
DR AlphaFoldDB; F2RAY6; -.
DR STRING; 953739.SVEN_5919; -.
DR GeneID; 69867963; -.
DR KEGG; sve:SVEN_5919; -.
DR PATRIC; fig|953739.5.peg.1131; -.
DR eggNOG; COG0155; Bacteria.
DR HOGENOM; CLU_015667_2_3_11; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000006854; Chromosome.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.480.20; -; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
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 PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32439:SF0; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CCA59205.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006854};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 101..164
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 172..327
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 349..414
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 425..562
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 62811 MW; EA878FA127BCD42B CRC64;
MAATPENPTP AAARRKTGRH RGEGQWAVGH FTPLNGNEQF KKDDDGLNVR TRIETVYSKR
GFDSIDPNDL RGRMRWWGLY TQRKQGLDGT KTGVLEPEEL DDEYFMLRVR IDGGRLTTEQ
LRVIGEISEE FARGTADITD RQNVQYHWIR IEDVPEIWNR LEAVGLSTTE ACGDTPRVIL
GSPVAGIAAD EIIDGTPAID EIYRRIVGNK DFSNLPRKFK SAVSGSPQLD VAHEINDIAF
VGVHHPEHGP GFDVWVGGGL STNPKLGVRL GAWVSLDEVP DVYEGVISIF RDYGYRRLRN
RARLKFLVAD WGPEKFRQVL EDEYLRRKLT DGPAPEQPAG QWRDHMGVHR QNDGRFYIGF
APRVGRVDGA TLTKIAALAE QHGSGRLRTT ADQKMILLDV EEAQLDSAVA ALEALDLRVN
PTPFRRGTMA CTGIEFCKLA IVETKARGAS LIDELERRVP DFDEPLTINI NGCPNACARI
QVADIGLKGQ LVLDGDGNRV EGYQVHLGGA LGLEAGFGRK VRGLKVTAAE LPDYVERVLK
RFQAERETGE RFATWAARAS EEALS
//
