NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 21371 / JCM 2853;
PubMed=8117070 [NCBI, ExPASy, EBI, Israel, Japan]
Motoyama H., Maki K., Anazawa H., Ishino S., Teshiba S.;
"Cloning and nucleotide sequences of the homoserine dehydrogenase genes (hom) and the threonine synthase genes (thrC) of the Gram-negative obligate methylotroph Methylobacillus glycogenes.";
Appl. Environ. Microbiol. 60:111-119(1994).

Comments

CATALYTIC ACTIVITY: L-homoserine + NAD(P)⁺ = L-aspartate 4-semialdehyde + NAD(P)H.
PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3 .
PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5 .
SIMILARITY: Belongs to the homoserine dehydrogenase family.
SIMILARITY: Contains 1 ACT domain.

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

D14071; BAA40415.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

P37144.

Family and domain databases

InterPro

IPR002912; ACT_bd.
IPR005106; Asp/hSer_DHase_NAD-bd.
IPR016204; hSer_DHase.
IPR001342; hSer_DHase_cat.
Graphical view of domain structure.

Pfam

PF01842; ACT; 1.
PF00742; Homoserine_dh; 1.
PF03447; NAD_binding_3; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000098; Homoser_dehydrog; 1.

PROSITE

PS01042; HOMOSER_DHGENASE; 1.

Other

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

Keywords

Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Isoleucine biosynthesis; Methionine biosynthesis; NADP; Oxidoreductase; Threonine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 412`	`412`	`Homoserine dehydrogenase.`	`PRO_0000066699`
`DOMAIN`	`329 404`	`76`	`ACT.`
`NP_BIND`	`9 16`	`8`	`NADP (By similarity).`
`ACT_SITE`	`205 205`		`Proton donor (Potential).`
`BINDING`	`105 105`		`NADP (By similarity).`
`BINDING`	`190 190`		`Substrate (By similarity).`

Sequence information

Length: 412 AA [This is the length of the unprocessed precursor]

Molecular weight: 44818 Da [This is the MW of the unprocessed precursor]

CRC64: 613A1B7FDECEF4AA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPINVGLLG IGTVGGGTYT VLTRNQEEIA RRAGRPIAIT RVADRNLELA RQVTGGKIDV 

        70         80         90        100        110        120 
TDDAFAIVSD PAIDIVVELI GGYTVARELV LKAIENGKHV VTANKALIAC MAMKFLPLRR 

       130        140        150        160        170        180 
KKASSSLLKL PLLVVSPLFK AVREGLAANR IEWIAGIING TTNFILSEMR EKGLAFADVL 

       190        200        210        220        230        240 
KEAQRLGYAE ADPTFDVEGI DAAHKLMILA AMLWLFVHSL CRGITKLDAV DITKRTDKGV 

       250        260        270        280        290        300 
ELRVHPTLIP EKRLICQCEW RNECCAGQGR CCWPTLYYGA GAGAEPTASA VADLVDGTDR 

       310        320        330        340        350        360 
GISCPHLAFQ PDRLVDLPIL PIGEISSAYY LRLRAVDKPG VLADVTRILG DRQISIDAMI 

       370        380        390        400        410 
QKEPQEGEDQ ADIIILTHVT VEKNMDDAIA AIEALPAISG KVTRLRMEEL SR

P37144 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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