DSVD_DESVH
ID DSVD_DESVH Reviewed; 78 AA.
AC Q46582;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protein DsvD;
GN Name=dsvD; OrderedLocusNames=DVU_0404;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7887608; DOI=10.1128/aem.61.1.290-296.1995;
RA Karkhoff-Schweizer R.R., Huber D.P.W., Voordouw G.;
RT "Conservation of the genes for dissimilatory sulfite reductase from
RT Desulfovibrio vulgaris and Archaeoglobus fulgidus allows their detection by
RT PCR.";
RL Appl. Environ. Microbiol. 61:290-296(1995).
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: May play an essential role in dissimilatory sulfite
CC reduction.
CC -!- SIMILARITY: To A.fulgidus DsrD. {ECO:0000305}.
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DR EMBL; U16723; AAA70109.1; -; Genomic_DNA.
DR EMBL; AE017285; AAS94887.1; -; Genomic_DNA.
DR RefSeq; WP_010937711.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009628.1; NC_002937.3.
DR PDB; 1UCR; X-ray; 1.20 A; A/B=1-78.
DR PDB; 1WQ2; Neutron; 2.40 A; A/B=1-78.
DR PDBsum; 1UCR; -.
DR PDBsum; 1WQ2; -.
DR AlphaFoldDB; Q46582; -.
DR SMR; Q46582; -.
DR IntAct; Q46582; 3.
DR STRING; 882.DVU_0404; -.
DR PaxDb; Q46582; -.
DR EnsemblBacteria; AAS94887; AAS94887; DVU_0404.
DR KEGG; dvu:DVU_0404; -.
DR PATRIC; fig|882.5.peg.381; -.
DR eggNOG; ENOG5033191; Bacteria.
DR HOGENOM; CLU_196901_0_0_7; -.
DR OMA; MVFWSSG; -.
DR EvolutionaryTrace; Q46582; -.
DR Proteomes; UP000002194; Chromosome.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR014793; DsrD.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF08679; DsrD; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT CHAIN 1..78
FT /note="Protein DsvD"
FT /id="PRO_0000080034"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1UCR"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1UCR"
FT HELIX 24..30
FT /evidence="ECO:0007829|PDB:1UCR"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:1UCR"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1UCR"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1UCR"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:1UCR"
SQ SEQUENCE 78 AA; 8830 MW; F4D10CBE7592FB0D CRC64;
MEEAKQKVVD FLNSKSGSKS KFYFNDFTDL FPDMKQREVK KILTALVNDE VLEYWSSGST
TMYGLKGAGK QAAAEHED
