Reviewed, UniProtKB/Swiss-Prot P77161 (GLXR_ECOLI)

Names and origin

Protein names

Recommended name:
    2-hydroxy-3-oxopropionate reductase
    EC=1.1.1.60
Alternative name(s):
    Tartronate semialdehyde reductase
      Short name=TSAR

Gene names

Name:	glxR
Synonyms:	glxB1, ybbQ
Ordered Locus Names:	b0509, JW0497

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	(R)-glycerate + NAD(P)(+) = 2-hydroxy-3-oxopropanoate + NAD(P)H.
Pathway	Organic acid metabolism; glycolic acid degradation; 3-phospho-D-glyceric acid from glycolic acid: step 3/4.
Induction	By glyoxylate.
Sequence similarities	Belongs to the 3-hydroxyisobutyrate dehydrogenase family.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glyoxylate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pentose-phosphate shunt Inferred from electronic annotation. Source: InterPro valine metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	2-hydroxy-3-oxopropionate reductase activity Inferred from electronic annotation. Source: InterPro 3-hydroxyisobutyrate dehydrogenase activity Inferred from electronic annotation. Source: InterPro coenzyme binding Inferred from electronic annotation. Source: InterPro phosphogluconate dehydrogenase (decarboxylating) activity 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 – 292	292	2-hydroxy-3-oxopropionate reductase		PRO_0000173061
Sites
	Active site	169	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P77161-1 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 5D5263231F2910F0	FASTA	292	30,801
	10 20 30 40 50 60 MKLGFIGLGI MGTPMAINLA RAGHQLHVTT IGPVADELLS LGAVSVETAR QVTEASDIIF 70 80 90 100 110 120 IMVPDTPQVE EVLFGENGCT KASLKGKTIV DMSSISPIET KRFARQVNEL GGDYLDAPVS 130 140 150 160 170 180 GGEIGAREGT LSIMVGGDEA VFERVKPLFE LLGKNITLVG GNGDGQTCKV ANQIIVALNI 190 200 210 220 230 240 EAVSEALLFA SKAGADPVRV RQALMGGFAS SRILEVHGER MIKRTFNPGF KIALHQKDLN 250 260 270 280 290 LALQSAKALA LNLPNTATCQ ELFNTCAANG GSQLDHSALV QALELMANHK LA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli." Cusa E., Obradors N., Baldoma L., Badia J., Aguilar J. J. Bacteriol. 181:7479-7484(1999) [PubMed: 10601204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: K12 / ECL1.
[2]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U89279 Genomic DNA. Translation: AAB93851.1. U82664 Genomic DNA. Translation: AAB40262.1. U00096 Genomic DNA. Translation: AAC73611.1. AP009048 Genomic DNA. Translation: BAE76287.1.
PIR	D64782.
RefSeq	AP_001157.1. NP_415042.1.
3D structure databases
SMR	P77161. Positions 1-291.
ModBase	Search...
Genome annotation databases
GeneID	945146.
GenomeReviews	Gene locus b0509 in contig U00096_GR. Gene locus JW0497 in contig AP009048_GR.
KEGG	ecj:JW0497. eco:b0509.
Organism-specific databases
EchoBASE	EB3052.
EcoGene	EG13265. glxR.
CMR	Search...
Phylogenomic databases
HOGENOM	P77161.
Enzyme and pathway databases
BioCyc	EcoCyc:G6278-MON. MetaCyc:G6278-MON.
Family and domain databases
InterPro	IPR002204. 3-OH-isobutyrate_DHase-rel_CS. IPR015815. 3hydroxyacid_DHase/Rdtase. IPR006183. 6-phosphogluconate_DHase. IPR006115. 6PGDH_NAD-bd. IPR013328. DHase_multihelical. IPR016040. NAD(P)-bd. IPR006398. Tartro_sem_red. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit.
PANTHER	PTHR22981. 3hydroxy_acid_DH. 1 hit.
Pfam	PF03446. NAD_binding_2. 1 hit. [Graphical view]
PRINTS	PR00076. 6PGDHDRGNASE.
TIGRFAMs	TIGR01505. tartro_sem_red. 1 hit.
PROSITE	PS00895. 3_HYDROXYISOBUT_DH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLXR_ECOLI

Accession

Primary (citable) accession number: P77161
Secondary accession number(s): Q2MBR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 1, 1997
Last modified:	November 25, 2008
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)