[1]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1016/0022-2836(94)90016-7; PubMed=8120891 [NCBI, ExPASy, EBI, Israel, Japan] Goldberg J.D., Yoshida T., Brick P.; "Crystal structure of a NAD-dependent D-glycerate dehydrogenase at 2.4-A resolution."; J. Mol. Biol. 236:1123-1140(1994).
[2]	CHARACTERIZATION. STRAIN=KM146 / GM2; PubMed=2114287 [NCBI, ExPASy, EBI, Israel, Japan] Izumi Y., Yoshida T., Kanzaki H., Toki S., Miyazaki S.S., Yamada H.; "Purification and characterization of hydroxypyruvate reductase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2."; Eur. J. Biochem. 190:279-284(1990).

Comments

FUNCTION: Active on hydroxypyruvate and glyoxylate.
CATALYTIC ACTIVITY: (R)-glycerate + NAD⁺ = hydroxypyruvate + NADH.
BIOPHYSICOCHEMICAL PROPERTIES:

pH dependence: Optimum pH is 6.8;
Temperature dependence: Optimum temperature is 45 degrees Celsius;
PATHWAY: One-carbon metabolism; formaldehyde assimilation via serine pathway .
SUBUNIT: Homodimer.
INDUCTION: By methanol.
SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

3D structure databases

PDB

1GDH; X-ray; 2.40 A; A/B=3-322.

[ExPASy / RCSB / EBI]

PDBsum

1GDH; -.

ModBase

P36234.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-4245; -.

Family and domain databases

InterPro

IPR006139; D-isomer_2_OHA_DHase.
IPR006140; D-isomer_2_OHA_DHase_NAD-bd.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

Pfam

PF00389; 2-Hacid_dh; 1.
PF02826; 2-Hacid_dh_C; 1.
Pfam graphical view of domain structure.

PROSITE

PS00065; D_2_HYDROXYACID_DH_1; 1.
PS00670; D_2_HYDROXYACID_DH_2; 1.
PS00671; D_2_HYDROXYACID_DH_3; 1.

Other

P36234; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; NAD; Oxidoreductase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 322`	`321`	`Glycerate dehydrogenase.`	`PRO_0000075942`
`REGION`	`2 100`	`99`	`Catalytic.`
`REGION`	`101 291`	`191`	`Coenzyme-binding.`
`REGION`	`292 322`	`31`	`Catalytic.`
`ACT_SITE`	`241 241`
`ACT_SITE`	`270 270`
`ACT_SITE`	`288 288`		`Proton donor.`
`STRAND`	`5 10`	`6`
`HELIX`	`14 21`	`8`
`STRAND`	`24 28`	`5`
`HELIX`	`37 44`	`8`
`STRAND`	`48 53`	`6`
`HELIX`	`60 65`	`6`
`STRAND`	`72 78`	`7`
`HELIX`	`85 90`	`6`
`STRAND`	`94 96`	`3`
`HELIX`	`103 118`	`16`
`HELIX`	`121 129`	`9`
`TURN`	`138 141`	`4`
`STRAND`	`150 154`	`5`
`HELIX`	`158 168`	`11`
`TURN`	`169 171`	`3`
`STRAND`	`173 177`	`5`
`HELIX`	`184 189`	`6`
`HELIX`	`198 204`	`7`
`STRAND`	`206 210`	`5`
`TURN`	`216 220`	`5`
`HELIX`	`224 227`	`4`
`STRAND`	`234 238`	`5`
`HELIX`	`242 244`	`3`
`HELIX`	`247 255`	`9`
`STRAND`	`258 265`	`8`
`TURN`	`268 271`	`4`
`HELIX`	`277 279`	`3`
`STRAND`	`283 285`	`3`
`HELIX`	`294 312`	`19`

Sequence information

Length: 322 AA [This is the length of the unprocessed precursor]

Molecular weight: 35115 Da [This is the MW of the unprocessed precursor]

CRC64: CA5E39C1617AF2FE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSKKKILITW PLPEAAMARA RESYDVIAHG DDPKITIDEM IETAKSVDAL LITLNEKCRK 

        70         80         90        100        110        120 
EVIDRIPENI KCISTYSIGF DHIDLDACKA RGIKVGNAPH GVTVATAEIA MLLLLGSARR 

       130        140        150        160        170        180 
AGEGEKMIRT RSWPGWEPLE LVGEKLDNKT LGIYGFGSIG QALAKRAQGF DMDIDYFDTH 

       190        200        210        220        230        240 
RASSSDEASY QATFHDSLDS LLSVSQFFSL NAPSTPETRY FFNKATIKSL PQGAIVVNTA 

       250        260        270        280        290        300 
RGDLVDNELV VAALEAGRLA YAGFDVFAGE PNINEGYYDL PNTFLFPHIG SAATQAREDM 

       310        320 
AHQANDLIDA LFGGADMSYA LA

P36234 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools