NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19, CHARACTERIZATION, AND SUBUNIT.
STRAIN=DSM 5473;
PubMed=11532010 [NCBI, ExPASy, EBI, Israel, Japan]
Ohshima T., Nunoura-Kominato N., Kudome T., Sakuraba H.;
"A novel hyperthermophilic archaeal glyoxylate reductase from Thermococcus litoralis. Characterization, gene cloning, nucleotide sequence and expression in Escherichia coli.";
Eur. J. Biochem. 268:4740-4747(2001).

Comments

CATALYTIC ACTIVITY: Glycolate + NAD⁺ = glyoxylate + NADH.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=0.73 mM for glyoxylate;
	K_M=1.3 mM for hydroxypyruvate;
	K_M=0.067 mM for NADH;
pH dependence:	Optimum pH is 6.5;
Temperature dependence:	Optimum temperature is 90 degrees Celsius. Extremely thermostable;

SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GyaR subfamily.

Copyright

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

Cross-references

Sequence databases

EMBL

AB033995; BAB40320.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P36234; 1GDH. [HSSP ENTRY / PDB]

SMR

Q9C4M5; 1-331.

ModBase

Q9C4M5.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0047964;	Molecular function: glyoxylate reductase activity (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00776; -; 1.
PBIL [Tree]

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

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

Keywords

Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 331`	`331`	`Glyoxylate reductase.`	`PRO_0000075951`
`NP_BIND`	`158 161`	`4`	`NADP (By similarity).`
`NP_BIND`	`180 182`	`3`	`NADP (By similarity).`
`NP_BIND`	`239 241`	`3`	`NADP (By similarity).`
`NP_BIND`	`288 290`	`3`	`NADP (By similarity).`
`ACT_SITE`	`241 241`		`By similarity.`
`ACT_SITE`	`270 270`		`By similarity.`
`ACT_SITE`	`288 288`		`Proton donor (By similarity).`

Sequence information

Length: 331 AA [This is the length of the unprocessed precursor]

Molecular weight: 36808 Da [This is the MW of the unprocessed precursor]

CRC64: E277D769D82B9763 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPKVFITRQ IPENGIKMIE KFYEIELWKD PKAPPRGVLL EKVREVDALV TLVTDKVDKE 

        70         80         90        100        110        120 
LLENAPKLKI IAQYAVGYDN IDIEEATKRG IYVTNTPGVL TDATADLAFA LLLAVARRIV 

       130        140        150        160        170        180 
EADAFVRSGE WKKSEVGWHP LMFLGYGLKG KTLGIVGFGR IGQALAKRAK GFGMKIIYYS 

       190        200        210        220        230        240 
RTRKPEAEEE IGAEYVDFET LLKESDFISL HVPLTKETYH MIGEKELKLM KPNAILINTS 

       250        260        270        280        290        300 
RGAVVDTNAL IKALKEGWIA GAGLDVFEEE PYYNEELFKL KNVVLAPHIG SATHEAREGM 

       310        320        330 
AELVAKNLIA FAKGEIPPNL VNKDVLTSSP P

Q9C4M5 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