HPSN_CUPPJ
ID HPSN_CUPPJ Reviewed; 436 AA.
AC Q46N53;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Sulfopropanediol 3-dehydrogenase;
DE EC=1.1.1.308 {ECO:0000269|PubMed:20150239};
DE AltName: Full=2,3-dihydroxypropane-1-sulfonate 3-dehydrogenase (sulfolactate forming);
DE Short=DHPS 3-dehydrogenase (sulfolactate forming);
GN Name=hpsN {ECO:0000303|PubMed:20150239}; OrderedLocusNames=Reut_C6092;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OG Plasmid megaplasmid Reut.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20150239; DOI=10.1099/mic.0.037580-0;
RA Mayer J., Huhn T., Habeck M., Denger K., Hollemeyer K., Cook A.M.;
RT "2,3-Dihydroxypropane-1-sulfonate degraded by Cupriavidus pinatubonensis
RT JMP134: purification of dihydroxypropanesulfonate 3-dehydrogenase.";
RL Microbiology 156:1556-1564(2010).
CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation of (R)-2,3-
CC dihydroxypropane-1-sulfonate to (R)-3-sulfolactate.
CC {ECO:0000269|PubMed:20150239}.
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:0000269|PubMed:20150239};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P06988};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P06988};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=160 uM for NAD(+) {ECO:0000269|PubMed:20150239};
CC KM=460 uM for (R)-2,3-dihydroxypropane-1-sulfonate
CC {ECO:0000269|PubMed:20150239};
CC Vmax=95 nmol/sec/mg enzyme {ECO:0000269|PubMed:20150239};
CC pH dependence:
CC Optimum pH is 9-10. {ECO:0000269|PubMed:20150239};
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; CP000092; AAZ65418.1; -; Genomic_DNA.
DR RefSeq; WP_011295860.1; NC_007336.1.
DR AlphaFoldDB; Q46N53; -.
DR SMR; Q46N53; -.
DR STRING; 264198.Reut_C6092; -.
DR EnsemblBacteria; AAZ65418; AAZ65418; Reut_C6092.
DR KEGG; reu:Reut_C6092; -.
DR eggNOG; COG0141; Bacteria.
DR HOGENOM; CLU_006732_3_0_4; -.
DR OMA; VCTPPDK; -.
DR OrthoDB; 935289at2; -.
DR BioCyc; MetaCyc:MON-15897; -.
DR BRENDA; 1.1.1.308; 11423.
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 1: Evidence at protein level;
KW Metal-binding; NAD; Oxidoreductase; Plasmid; Zinc.
FT CHAIN 1..436
FT /note="Sulfopropanediol 3-dehydrogenase"
FT /id="PRO_0000135827"
FT ACT_SITE 318
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06988, ECO:0000255|HAMAP-
FT Rule:MF_02228"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P06988, ECO:0000255|HAMAP-
FT Rule:MF_02228"
FT BINDING 118
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06988, ECO:0000255|HAMAP-
FT Rule:MF_02228"
FT BINDING 180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06988, ECO:0000255|HAMAP-
FT Rule:MF_02228"
FT BINDING 203
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P06988, ECO:0000255|HAMAP-
FT Rule:MF_02228"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988, ECO:0000255|HAMAP-
FT Rule:MF_02228"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988, ECO:0000255|HAMAP-
FT Rule:MF_02228"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988, ECO:0000255|HAMAP-
FT Rule:MF_02228"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P06988, ECO:0000255|HAMAP-
FT Rule:MF_02228"
SQ SEQUENCE 436 AA; 46881 MW; E505337929A7046C CRC64;
MISYLKKAEK TPQTETATAQ KVVTEMLAEI QARGKDAVRQ YAKQLDGWSG DIVLTPDQIR
EQTKDVPAGV RADIDFAIRQ VTDFALAQRE SLKEFSVELH PGVTAGQRVL PVNVVGCYAP
AGRYAHIASA YMGVATAKAA GVKTVVACSS PFRGQGIHPH VLYAFQAAGA DVIMALGGVQ
AIASMAYGLF TGKPADVVVG PGNKFVAEAK RSLYGQVGID VFAGPSEVAV IADETADPAI
VASDLVGQAE HGHESPAWLF TTSRDLADRV MALVPELIAK LPPTARDAAT AAWRDYGEVI
LCGTREEVVE ISDRYASEHL EVHTADLDWW LANLTCYGSL FLGEETTVAF GDKTSGPNHV
LPTKGAARYS GGLSVHKFMK TLTWQQMTRE ATRQIGQVTA RISRLEGMEA HARTADDRMA
KYFPNASFEM GTPVEV
