HPSN_RUEPO
ID HPSN_RUEPO Reviewed; 435 AA.
AC Q5LVV1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Sulfopropanediol 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02228};
DE EC=1.1.1.308 {ECO:0000255|HAMAP-Rule:MF_02228};
DE AltName: Full=2,3-dihydroxypropane-1-sulfonate 3-dehydrogenase (sulfolactate forming) {ECO:0000255|HAMAP-Rule:MF_02228};
DE Short=DHPS 3-dehydrogenase (sulfolactate forming) {ECO:0000255|HAMAP-Rule:MF_02228};
GN Name=hpsN {ECO:0000255|HAMAP-Rule:MF_02228}; OrderedLocusNames=SPO0594;
OS Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS pomeroyi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=246200;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=15602564; DOI=10.1038/nature03170;
RA Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT environment.";
RL Nature 432:910-913(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA Rivers A.R., Smith C.B., Moran M.A.;
RT "An updated genome annotation for the model marine bacterium Ruegeria
RT pomeroyi DSS-3.";
RL Stand. Genomic Sci. 9:11-11(2014).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of (R)-2,3-
CC dihydroxypropane-1-sulfonate to (R)-3-sulfolactate. {ECO:0000255|HAMAP-
CC Rule:MF_02228}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-sulfopropanediol + H2O + 2 NAD(+) = (2R)-3-sulfolactate
CC + 3 H(+) + 2 NADH; Xref=Rhea:RHEA:28074, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58738, ChEBI:CHEBI:60997; EC=1.1.1.308;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02228};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02228};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_02228};
CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. HpsN
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02228, ECO:0000305}.
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DR EMBL; CP000031; AAV93909.1; -; Genomic_DNA.
DR RefSeq; WP_011046350.1; NC_003911.12.
DR AlphaFoldDB; Q5LVV1; -.
DR SMR; Q5LVV1; -.
DR STRING; 246200.SPO0594; -.
DR EnsemblBacteria; AAV93909; AAV93909; SPO0594.
DR KEGG; sil:SPO0594; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_3_5; -.
DR OMA; MKIVTWQ; -.
DR OrthoDB; 935289at2; -.
DR Proteomes; UP000001023; Chromosome.
DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro.
DR CDD; cd06572; Histidinol_dh; 1.
DR HAMAP; MF_02228; Sulfopropanediol_dehydrog; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR001692; Histidinol_DH_CS.
DR InterPro; IPR022695; Histidinol_DH_monofunct.
DR InterPro; IPR012131; Hstdl_DH.
DR InterPro; IPR043678; Sulfopropanediol_dehydrog_HpsN.
DR PANTHER; PTHR21256; PTHR21256; 1.
DR Pfam; PF00815; Histidinol_dh; 1.
DR PIRSF; PIRSF000099; Histidinol_dh; 1.
DR PRINTS; PR00083; HOLDHDRGNASE.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR00069; hisD; 1.
DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1.
PE 3: Inferred from homology;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..435
FT /note="Sulfopropanediol 3-dehydrogenase"
FT /id="PRO_0000135846"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02228"
FT ACT_SITE 320
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02228"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02228"
FT BINDING 181
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02228"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02228"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02228"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02228"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02228"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02228"
SQ SEQUENCE 435 AA; 46644 MW; 093DF7F337198357 CRC64;
MTIEYLKKAS LTSKSDASDV QETVRAILAD IEAGGDQVAL DYAAKFDRYE GSIILSPEEI
EAACAKVPEK LKADIRFAHD NVRRFAETQK ATLTDVELEV VPGVITGQKA IPVDAAGCYV
PGGRYSHIAS AIMTVTTAKV AGCKHIMACS PPRPGVGVAP AIVYAAHICG ADTIMAIGGV
QGVASMAFGL FGLPKAKILV GPGNQFVAEA KRMLFGRVGI DMIAGPTDSL ILADRTADPH
IVTTDLVSQA EHGYNSPVWL VTDDRALAEK VIEMIPSYIA DLPEVNRDNA AAAWRDYAEV
ILCADREEMA ATSDRYAPEH LTVMAEDLDW WLDRLSCYGS LFLGEESTVS YGDKAAGTNH
VLPTSGAASY TGGLSVHKYM KIVTWQRGTR EGYKPVAEAT ARIARLEGME GHARAADVRL
AKYFPDETFD LTANG
