Q46N53 (HPSN_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sulfopropanediol 3-dehydrogenase
EC=1.1.1.308

Alternative name(s):
2,3-dihydroxypropane-1-sulfonate 3-dehydrogenase (sulfolactate forming)
Short name=DHPS 3-dehydrogenase (sulfolactate forming)

Gene names

Name:	hpsN
Ordered Locus Names:	Reut_C6092

Encoded on

Plasmid megaplasmid Reut

Organism

Cupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]

Taxonomic identifier

264198 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NAD-dependent oxidation of (R)-2,3-dihydroxypropane-1-sulfonate to (R)-3-sulfolactate. Ref.2
Catalytic activity	(R)-2,3-dihydroxypropane-1-sulfonate + 2 NAD+ + H2O = (R)-3-sulfolactate + 2 NADH. Ref.2
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_01024
Sequence similarities	Belongs to the histidinol dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=160 µM for NAD+ Ref.2 KM=460 µM for (R)-2,3-dihydroxypropane-1-sulfonate Vmax=95 nmol/sec/mg enzyme pH dependence: Optimum pH is 9-10.

Ontologies

Keywords
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Plasmid
Gene Ontology (GO)
Biological process	histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAD binding Inferred from electronic annotation. Source: InterPro histidinol dehydrogenase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 436	436	Sulfopropanediol 3-dehydrogenase HAMAP MF_01024		PRO_0000135827
Sites
	Active site	318	1	Proton acceptor By similarity
	Active site	319	1	Proton acceptor By similarity
	Metal binding	248	1	Zinc By similarity
	Metal binding	251	1	Zinc By similarity
	Metal binding	352	1	Zinc By similarity
	Metal binding	411	1	Zinc By similarity
	Binding site	118	1	NAD By similarity
	Binding site	180	1	NAD By similarity
	Binding site	203	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q46N53 [UniParc]. Last modified September 13, 2005. Version 1. Checksum: E505337929A7046C	FASTA	436	46,881
	10 20 30 40 50 60 MISYLKKAEK TPQTETATAQ KVVTEMLAEI QARGKDAVRQ YAKQLDGWSG DIVLTPDQIR 70 80 90 100 110 120 EQTKDVPAGV RADIDFAIRQ VTDFALAQRE SLKEFSVELH PGVTAGQRVL PVNVVGCYAP 130 140 150 160 170 180 AGRYAHIASA YMGVATAKAA GVKTVVACSS PFRGQGIHPH VLYAFQAAGA DVIMALGGVQ 190 200 210 220 230 240 AIASMAYGLF TGKPADVVVG PGNKFVAEAK RSLYGQVGID VFAGPSEVAV IADETADPAI 250 260 270 280 290 300 VASDLVGQAE HGHESPAWLF TTSRDLADRV MALVPELIAK LPPTARDAAT AAWRDYGEVI 310 320 330 340 350 360 LCGTREEVVE ISDRYASEHL EVHTADLDWW LANLTCYGSL FLGEETTVAF GDKTSGPNHV 370 380 390 400 410 420 LPTKGAARYS GGLSVHKFMK TLTWQQMTRE ATRQIGQVTA RISRLEGMEA HARTADDRMA 430 KYFPNASFEM GTPVEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence of a megaplasmid of Ralstonia eutropha JMP134." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Vergez L., Larimer F., Land M., Lykidis A., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: JMP134 / LMG 1197.
[2]	"2,3-Dihydroxypropane-1-sulfonate degraded by Cupriavidus pinatubonensis JMP134: purification of dihydroxypropanesulfonate 3-dehydrogenase." Mayer J., Huhn T., Habeck M., Denger K., Hollemeyer K., Cook A.M. Microbiology 156:1556-1564(2010) [PubMed: 20150239] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000092 Genomic DNA. Translation: AAZ65418.1.
RefSeq	YP_293275.1. NC_007336.1.
3D structure databases
ProteinModelPortal	Q46N53.
ModBase	Search...
Protein-protein interaction databases
STRING	Q46N53.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3607398.
GenomeReviews	Gene locus Reut_C6092 in contig CP000092_GR.
KEGG	reu:Reut_C6092.
NMPDR	fig|264198.3.peg.6.
PATRIC	20224618. VBIRalEut24049_0189.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG329596.
OMA	CYGSLFL.
ProtClustDB	PRK12447.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-15897. REUT264198:REUT_C6092-MONOMER.
Family and domain databases
HAMAP	MF_01024. HisD. Divergent sequence. [Tree]
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR001692. Histidinol_DH_CS. IPR022695. Histidinol_DH_monofunct. IPR012131. Hstdl_DH. [Graphical view]
KO	K15509.
PANTHER	PTHR21256:SF2. Hstdl_DH_prok. 1 hit.
Pfam	PF00815. Histidinol_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000099. Histidinol_dh. 1 hit.
PRINTS	PR00083. HOLDHDRGNASE.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR00069. HisD. 1 hit.
PROSITE	PS00611. HISOL_DEHYDROGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HPSN_CUPPJ

Accession

Primary (citable) accession number: Q46N53

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	September 13, 2005
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program