SOEA_ALLVD
ID SOEA_ALLVD Reviewed; 967 AA.
AC D3RNN8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Sulfite dehydrogenase subunit A {ECO:0000305};
DE EC=1.8.5.6 {ECO:0000269|PubMed:24030319};
DE AltName: Full=Sulfite dehydrogenase molybdopterin subunit {ECO:0000305};
DE AltName: Full=Sulfite-oxidizing enzyme subunit A {ECO:0000305};
GN Name=soeA {ECO:0000303|PubMed:24030319};
GN OrderedLocusNames=Alvin_2491 {ECO:0000312|EMBL:ADC63403.1};
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=24030319; DOI=10.1099/mic.0.071019-0;
RA Dahl C., Franz B., Hensen D., Kesselheim A., Zigann R.;
RT "Sulfite oxidation in the purple sulfur bacterium Allochromatium vinosum:
RT identification of SoeABC as a major player and relevance of SoxYZ in the
RT process.";
RL Microbiology 159:2626-2638(2013).
CC -!- FUNCTION: Part of the SoeABC complex that catalyzes the oxidation of
CC sulfite to sulfate. {ECO:0000269|PubMed:24030319}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H2O + sulfite = a quinol + sulfate;
CC Xref=Rhea:RHEA:50760, ChEBI:CHEBI:15377, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.8.5.6;
CC Evidence={ECO:0000269|PubMed:24030319};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a menaquinone + H2O + sulfite = a menaquinol + sulfate;
CC Xref=Rhea:RHEA:57012, Rhea:RHEA-COMP:9537, Rhea:RHEA-COMP:9539,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16189, ChEBI:CHEBI:16374,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:18151;
CC Evidence={ECO:0000269|PubMed:24030319};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P18775};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P18775};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250|UniProtKB:P18775};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250|UniProtKB:P18775};
CC -!- SUBUNIT: Forms a heterotrimeric membrane-bound complex composed of a
CC catalytic heterodimer (SoeAB) and a membrane anchor protein (SoeC).
CC {ECO:0000305|PubMed:24030319}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:24030319}; Peripheral membrane protein
CC {ECO:0000305|PubMed:24030319}; Cytoplasmic side
CC {ECO:0000305|PubMed:24030319}. Note=Attached to the membrane by
CC interaction with SoeC. {ECO:0000305|PubMed:24030319}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene causes a strong decrease in
CC sulfite oxidation rate. {ECO:0000269|PubMed:24030319}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; CP001896; ADC63403.1; -; Genomic_DNA.
DR RefSeq; WP_012971673.1; NC_013851.1.
DR AlphaFoldDB; D3RNN8; -.
DR SMR; D3RNN8; -.
DR STRING; 572477.Alvin_2491; -.
DR EnsemblBacteria; ADC63403; ADC63403; Alvin_2491.
DR KEGG; alv:Alvin_2491; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; LMHNVIT; -.
DR OrthoDB; 88184at2; -.
DR BioCyc; MetaCyc:MON-18521; -.
DR BRENDA; 1.8.5.6; 257.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 2.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Molybdenum; Oxidoreductase; Reference proteome.
FT CHAIN 1..967
FT /note="Sulfite dehydrogenase subunit A"
FT /id="PRO_0000446046"
FT DOMAIN 15..71
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
SQ SEQUENCE 967 AA; 108956 MW; E32CDD322F0868F1 CRC64;
MQDPASHSDS LVGRVEVKET TCYMCACRCG IRVHLRDGEV RYIDGNPNHP LNKGVICAKG
SSGIMKQYSP GRLTQPLRRK AGAERGESAF EVISWDEAFA MLEERLAKLR AEDPKKFALF
TGRDQMQALT GLFAKQYGTP NYAAHGGFCS VNMAAGLIYT IGGSFWEFGG PDLERAKLFV
MIGTAEDHHS NPLKMAISEF KRRGGRFISV NPVRTGYSAV ADEWVPIKPG TDGALLLAIT
REILDKGLFD RDFLVRYTNA AELVIDDPSR DDHGLFYRAE MHVEPDCFDP QNKLWWDRDI
DGPISTHTPG ADPRLMGRYV LPDGTPVKPS FQLLKERLEQ YTPEWAAPIT GIPADTIRRL
AHEMGVMARD QKIELPIKWT DCWDDEHESV TGNPVAFHAM RGLAAHSNGF QTIRALGVLM
TVLGTIDRPG GFRHKAPYPR PIPPCPKPPH GPEAVQPNTP LDGMPLGWPS KPEDLFVDAE
GEAVRLDKAF SWEYPLSVHG LMHNVITNAW RGDPYPIDTL FLFMANMAWN STMNTVEVRK
MLVDKHPNGD YKIPFLVVCD TFASETVAFA DLVLPDTSYL ERHDVLSMLD RPISEFDGPV
DSVRIPVLPP KGECKPFQEV LVELGSRLKL PAFTNADGSR KYRNYPDFIV NYETSPGSGI
GFLAGWRGKG GDQFLKGEPN PHQWEMYAQN NCVYHHELPR SYQYMRNWNK GYLHWARAHG
MIRYAEPITL HLYSEVLQRF RLAAQGKRPG RQPPERLRQR VETYFDPLPF YYEPLESRFT
DTQRYPLNAL TQRPMAMYHS WDSQNAWLRQ IHSHNYLFLS PKVGLAQGFA DGDWVWVESP
HGKVRCMCRF SEAVEPGTVW TWNAIGKGAG AWGLAPNADE ARKGFLLNHV IAEELPAHEA
GEHLSNSDPV TGQAAWFDVR VRVYKAEAGE PEVTSPQFKP MPRLPGQEKK RGKWQAYVAG
IFGKQAS
