ID A0A318LG39_9PSEU Unreviewed; 560 AA.
AC A0A318LG39;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=BA062_31125 {ECO:0000313|EMBL:PXY21990.1};
OS Prauserella flavalba.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Prauserella.
OX NCBI_TaxID=1477506 {ECO:0000313|EMBL:PXY21990.1, ECO:0000313|Proteomes:UP000247892};
RN [1] {ECO:0000313|EMBL:PXY21990.1, ECO:0000313|Proteomes:UP000247892}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 121212 {ECO:0000313|EMBL:PXY21990.1,
RC ECO:0000313|Proteomes:UP000247892};
RA Ruckert C., Albersmeier A., Jiang C.-L., Jiang Y., Kalinowski J.,
RA Schneider O., Winkler A., Zotchev S.B.;
RT "Draft genome sequence of Prauserella sp. YIM 121212, isolated from
RT alkaline soil.";
RL Submitted (JUL-2016) 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};
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:PXY21990.1}.
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DR EMBL; MASU01000014; PXY21990.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318LG39; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000247892; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000247892};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 95..157
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 166..319
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 340..406
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 417..556
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 61890 MW; 10CFD04C51E8A19A CRC64;
MAPNAGRPAR TKQRRGEGQW ALGYREPLNP NERSKKDDHP LNVRARIENI YARGGFDSID
PGDLRGRFRW YGLYTQRKPG IDGGRTATLE PEELDDSYFM LRVRLDGGAL TTDQLALLGE
ISQTYARDTA DITDRQNIQY HWIQVEDMPT IWKKLEDAGL TTMEACGDSP RVILGSPVAG
ISKDEVIDGT PAIEEIRRRY VGDPQFANLP RKFKTAISGQ QDVAHEIHDV AFVGVEHPEH
GPGFDVWVGG GLSTNPMIAQ RLGAWVPLDE VPEVWAGVIG IFRDYGYRRL RSRARIKFLV
KDWGAEKFRE VLETEYLKRP LIDGPAPEVP ERPIDHIGVH QQKDGLYYVG GAPVAGRSSG
SMLIAAAKAA ERAGSGRVRL TPQQKLVVLD VPETEVDGLK AELAEAGLQT EPSPWRRNVM
ACTGIEFCKL AIVETKARAE ALVAELEQRL AGIQDGLDNP VTVHLNGCPN SCARIQVADI
GLKGQIVTDD EGNQVEGFQV HLGGGLGLDA GFGRKLRGHK VTSAELTDYV ERVVRNYLAG
REDGERFAQW VTRAEEAELK
//
