Reviewed, UniProtKB/Swiss-Prot P08499 (DHOM_CORGL)

Names and origin

Protein names

Recommended name:
    Homoserine dehydrogenase
      Short name=HDH
    EC=1.1.1.3

Gene names

Name:	hom
Synonyms:	thrA
Ordered Locus Names:	Cgl1183, cg1337

Organism

Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.
Enzyme regulation	Feedback inhibition by threonine.
Pathway	Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.
Sequence similarities	Belongs to the homoserine dehydrogenase family. Contains 1 ACT domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis Methionine biosynthesis Threonine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro amino acid binding Inferred from electronic annotation. Source: InterPro homoserine dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 445	445	Homoserine dehydrogenase		PRO_0000066693
Regions
	Domain	367 – 439	73	ACT
	Nucleotide binding	24 – 31	8	NADP By similarity
Sites
	Active site	219	1	Proton donor Potential
	Binding site	119	1	NADP By similarity
	Binding site	204	1	Substrate By similarity
Natural variations
	Natural variant	378	1	G → E in FBR mutant.

Sequences

	Sequence		Length	Mass (Da)
	P08499-1 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 02731E502303CB1C	FASTA	445	46,438
	10 20 30 40 50 60 MTSASAPSFN PGKGPGSAVG IALLGFGTVG TEVMRLMTEY GDELAHRIGG PLEVRGIAVS 70 80 90 100 110 120 DISKPREGVA PELLTEDAFA LIEREDVDIV VEVIGGIEYP REVVLAALKA GKSVVTANKA 130 140 150 160 170 180 LVAAHSAELA DAAEAANVDL YFEAAVAGAI PVVGPLRRSL AGDQIQSVMG IVNGTTNFIL 190 200 210 220 230 240 DAMDSTGADY ADSLAEATRL GYAEADPTAD VEGHDAASKA AILASIAFHT RVTADDVYCE 250 260 270 280 290 300 GISNISAADI EAAQQAGHTI KLLAICEKFT NKEGKSAISA RVHPTLLPVS HPLASVNKSF 310 320 330 340 350 360 NAIFVEAEAA GRLMFYGNGA GGAPTASAVL GDVVGAARNK VHGGRAPGES TYANLPIADF 370 380 390 400 410 420 GETTTRYHLD MDVEDRVGVL AELASLFSEQ GISLRTIRQE ERDDDARLIV VTHSALESDL 430 440 SRTVELLKAK PVVKAINSVI RLERD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and fine structural analysis of the Corynebacterium glutamicum hom-thrB operon." Peoples O.P., Liebl W., Bodis M., Maeng P.J., Follettie M.T., Archer J.A.C., Sinskey A.J. Mol. Microbiol. 2:63-72(1988) [PubMed: 2835591] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[2]	"Nucleotide sequence of the homoserine dehydrogenase (thr A) gene of Brevibacterium lactofermentum." Mateos L.M., del Real G., Aguilar A., Martin J.F. Nucleic Acids Res. 15:10598-10598(1987) [PubMed: 3320973] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence analysis of functional regions of homoserine dehydrogenase genes from L-lysine and L-threonine-producing mutants of Brevibacterium lactofermentum." Sugimoto M., Tanaka A., Suzuki T., Matsui H., Nakamori S., Takagi H. Biosci. Biotechnol. Biochem. 61:1760-1762(1997) [PubMed: 9362124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[5]	"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[6]	"Analysis of a Corynebacterium glutamicum hom gene coding for a feedback-resistant homoserine dehydrogenase." Reinscheid D.J., Eikmanns B.J., Sahm H. J. Bacteriol. 173:3228-3230(1991) [PubMed: 1902466] [Abstract] Cited for: MUTANT RESISTANT TO FEEDBACK INHIBITION (FBR).

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y00546 Genomic DNA. Translation: CAA68614.1. Y00476 Genomic DNA. Translation: CAA68536.1. BA000036 Genomic DNA. Translation: BAB98576.1. BX927151 Genomic DNA. Translation: CAF19887.1.
PIR	DEFKHG. S00865.
RefSeq	NP_600409.1. YP_225473.1.
3D structure databases
ModBase	Search...
2-D gel databases
World-2DPAGE	0001:P08499.
Proteomic databases
PRIDE	P08499.
Genome annotation databases
GeneID	1019166. 3343957.
GenomeReviews	Gene locus Cgl1183 in contig BA000036_GR. Gene locus cg1337 in contig BX927147_GR.
KEGG	cgb:cg1337. cgl:NCgl1136.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P08499.
OMA	P08499. LGIVNGT.
Enzyme and pathway databases
BioCyc	CGLU196627-1:CG1337-MON.
BRENDA	1.1.1.3. 812.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR005106. Asp/hSer_DH_NAD-bd. IPR016204. Homoserine_dehydrogenase. IPR001342. Homoserine_dehydrogenase_cat. IPR019811. Homoserine_dehydrogenase_CS. [Graphical view]
Pfam	PF01842. ACT. 1 hit. PF00742. Homoserine_dh. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
PIRSF	PIRSF000098. Homoser_dehydrog. 1 hit.
PROSITE	PS01042. HOMOSER_DHGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHOM_CORGL

Accession

Primary (citable) accession number: P08499

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 74 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)