SOEB_ALLVD
ID SOEB_ALLVD Reviewed; 240 AA.
AC D3RNN7;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Sulfite dehydrogenase subunit B {ECO:0000305};
DE AltName: Full=Sulfite dehydrogenase iron-sulfur subunit {ECO:0000305};
DE AltName: Full=Sulfite-oxidizing enzyme subunit B {ECO:0000305};
GN Name=soeB {ECO:0000303|PubMed:24030319};
GN OrderedLocusNames=Alvin_2490 {ECO:0000312|EMBL:ADC63402.1};
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, SUBUNIT, AND SUBCELLULAR LOCATION.
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. SoeB is probably the electron transfer subunit.
CC {ECO:0000269|PubMed:24030319}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 3 [4Fe-4S] clusters. {ECO:0000255|PROSITE-ProRule:PRU00711};
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}.
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DR EMBL; CP001896; ADC63402.1; -; Genomic_DNA.
DR RefSeq; WP_012971672.1; NC_013851.1.
DR AlphaFoldDB; D3RNN7; -.
DR SMR; D3RNN7; -.
DR STRING; 572477.Alvin_2490; -.
DR EnsemblBacteria; ADC63402; ADC63402; Alvin_2490.
DR KEGG; alv:Alvin_2490; -.
DR eggNOG; COG0437; Bacteria.
DR HOGENOM; CLU_043374_1_1_6; -.
DR OMA; EKCTWCY; -.
DR OrthoDB; 1762646at2; -.
DR BioCyc; MetaCyc:MON-18522; -.
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 InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR Pfam; PF13247; Fer4_11; 1.
DR Pfam; PF12800; Fer4_4; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 1: Evidence at protein level;
KW 4Fe-4S; Cell inner membrane; Cell membrane; Electron transport; Iron;
KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..240
FT /note="Sulfite dehydrogenase subunit B"
FT /id="PRO_0000446047"
FT DOMAIN 4..34
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 64..95
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 97..126
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 13
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 16
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 76
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 106
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 116
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 240 AA; 26995 MW; 18F8EAE744ECC48E CRC64;
MTQLALVIDL NVCVGCHACV TSCKEWNTSG WAGPLVDQNP YEGSPTGTFF NRVQTFEIGT
FPNTETVHFP KSCLHCEEPP CVPVCPTGAS YKRPDNGVVL VDYDKCIGCK YCSWACPYGA
RELDAQQKVM KKCTLCIDRI TDAKLSERDR KPSCVLACPA NARLFGDVHD PDSEVSIAIR
ERGGYQLMPE WGTKPANHYL PRRKTRMHID PEELTRVDNP WRKEDLTDYT GEETLDDVAW
