ID HMC6_DESVH Reviewed; 461 AA.
AC P33393;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Protein DVU_0531;
DE AltName: Full=HMC operon ORF 6;
GN OrderedLocusNames=DVU_0531;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8335628; DOI=10.1128/jb.175.15.4699-4711.1993;
RA Rossi M., Pollock W.B.R., Reij M.W., Keon R.G., Fu R., Voordouw G.;
RT "The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough
RT encodes a potential transmembrane redox protein complex.";
RL J. Bacteriol. 175:4699-4711(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
CC -!- FUNCTION: HMWC (high-molecular-weight cytochrome c precursor), ORF2,
CC ORF3, ORF4, ORF5, ORF6 in the HMC operon form a transmembrane protein
CC complex that allows electron flow from the periplasmic hydrogenase to
CC the cytoplasmic enzymes that catalyze reduction of sulfates. ORF6 is a
CC redox protein.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR EMBL; L16784; AAA71999.1; -; Unassigned_DNA.
DR EMBL; AE017285; AAS95013.1; -; Genomic_DNA.
DR PIR; F40605; F40605.
DR RefSeq; WP_010937837.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009754.1; NC_002937.3.
DR AlphaFoldDB; P33393; -.
DR STRING; 882.DVU_0531; -.
DR PaxDb; 882-DVU_0531; -.
DR EnsemblBacteria; AAS95013; AAS95013; DVU_0531.
DR KEGG; dvu:DVU_0531; -.
DR PATRIC; fig|882.5.peg.507; -.
DR eggNOG; COG0247; Bacteria.
DR HOGENOM; CLU_023081_6_0_7; -.
DR OrthoDB; 9786127at2; -.
DR PhylomeDB; P33393; -.
DR BioCyc; MetaCyc:MONOMER-22167; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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 Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004017; Cys_rich_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43551; FUMARATE REDUCTASE IRON-SULFUR SUBUNIT; 1.
DR PANTHER; PTHR43551:SF1; HETERODISULFIDE REDUCTASE; 1.
DR Pfam; PF02754; CCG; 1.
DR Pfam; PF13534; Fer4_17; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
PE 4: Predicted;
KW 4Fe-4S; Cytoplasm; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..461
FT /note="Protein DVU_0531"
FT /id="PRO_0000159256"
FT DOMAIN 54..84
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 112..140
FT /note="4Fe-4S ferredoxin-type 2"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 461 AA; 52730 MW; 21EC00F1984D0A7C CRC64;
MPEGKFCNRK PVNTEEDLKA LLGDKGGAQY YKEMEELEVD QEALWANIEK TCQSRTKTWL
EICAHCGMCA DSCFLYRVND RDPKQVPAYK IQSTLGEIIR RKGKVDTQFM LHAMEVAWSQ
CTCCNRCGQY CPHGIDMGVM FSYLRGLLYS QGFVPWELKI GSGMHRVYGA QMDVTTEDWV
ETCEWMAEEQ QEEWPGLEIP VDVENADIMY VLNAREPKHY PEDVAEAAIL FHIAGENWTV
PSEGWEQTSL AMFAGDWAAC KMQVERVYAA IERLKPKCVV GTECGHAHRA SAIEGPYWAG
YEDGKTPAPW LHYVEWVAMA LRTGKIKIDP EKRIKEPVTL QDSCNYIRNH GLAKCTREIM
SYIADDFREM TPNREHNYCC GGGGGFNGIG KFRKQRNKAL QTKRDQILAT GAKLVVAPCH
NCWDAIRDLE EEYRIGIRWS FLKPLIIKMA IIPEHLRPEE E
//
