DSVA_MEGG1
ID DSVA_MEGG1 Reviewed; 198 AA.
AC P94693;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Sulfite reductase, dissimilatory-type subunit alpha;
DE AltName: Full=Desulfoviridin subunit alpha;
DE AltName: Full=Dissimilatory sulfite reductase subunit alpha;
DE Short=dSiR alpha;
DE AltName: Full=Hydrogensulfite reductase subunit alpha;
DE Flags: Fragment;
GN Name=dsrA;
OS Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM
OS B-1759) (Desulfovibrio gigas).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=1121448;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759;
RA Hipp W.M., Trueper H.G.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the complex that catalyzes the reduction of sulfite
CC to sulfide. The alpha and beta subunits may have arisen by gene
CC duplication. They both bind 2 iron-sulfur clusters, but the alpha
CC subunit seems to be catalytically inactive, due to substitutions along
CC the putative substrate access channel, and because it binds
CC sirohydrochlorin (the dematallated form of siroheme) instead of
CC siroheme. {ECO:0000250|UniProtKB:P45574}.
CC -!- SUBUNIT: Heterohexamer of two alpha, two beta and two gamma subunits.
CC {ECO:0000250|UniProtKB:P45574}.
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DR EMBL; U80961; AAB41001.1; -; Genomic_DNA.
DR AlphaFoldDB; P94693; -.
DR SMR; P94693; -.
DR STRING; 1121448.DGI_0691; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.413.10; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR PANTHER; PTHR11493; PTHR11493; 1.
DR Pfam; PF01077; NIR_SIR; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding.
FT CHAIN <1..198
FT /note="Sulfite reductase, dissimilatory-type subunit alpha"
FT /id="PRO_0000080029"
FT DOMAIN 55..83
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45574"
FT BINDING 64
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45574"
FT BINDING 67
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45574"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P45574"
FT NON_TER 1
SQ SEQUENCE 198 AA; 22384 MW; 92B9643231A98AE4 CRC64;
WKDDIKIDQE AVKAYVGGEF KPNAGAHAGR DWGKFDIEAE VVGLCPTGCM TYESGTLSID
NKNCTRCMHC INTMPRALKI GDERGASILV GAKAPVLDGA QMGSLLIPFI AAEEPFDEVK
EVIENIWEWW MEEGKNRERL GETMKRVGFQ KLLEVTGTKA VPQHVSEPRH NPYIFFKEEE
VPGGWSRDIS DYRKRHMR
