NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MG1614;
PubMed=8682767 [NCBI, ExPASy, EBI, Israel, Japan]
Madsen S.M., Albrechtsen B., Hansen E.B., Israelsen H.;
"Cloning and transcriptional analysis of two threonine biosynthetic genes from Lactococcus lactis MG1614.";
J. Bacteriol. 178:3689-3694(1996).

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

X96988; CAA65713.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC6049; JC6049.

3D structure databases

ModBase

P52985.

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`	`1 428`	`428`	`Homoserine dehydrogenase.`	`PRO_0000066697`
`DOMAIN`	`350 423`	`74`	`ACT.`
`NP_BIND`	`8 15`	`8`	`NADP (By similarity).`
`ACT_SITE`	`206 206`		`Proton donor (Potential).`
`BINDING`	`106 106`		`NADP (By similarity).`
`BINDING`	`191 191`		`Substrate (By similarity).`

Sequence information

Length: 428 AA [This is the length of the unprocessed precursor]

Molecular weight: 46629 Da [This is the MW of the unprocessed precursor]

CRC64: B178CF30D62A6349 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVNIAILGF GTVGTGLPTL LSENKEKLAK ILDEEIVISK VLMRDNKAIE KARSQGFNYD 

        70         80         90        100        110        120 
FVLNLDDILA DSEISIVVEL MGRIEPAKTY ITQAIEAGKN VVTANKDLLA VHGVELRSLA 

       130        140        150        160        170        180 
QKHHVALYYE AAVAGGIPIL RTLANSFSSD KITHLLGILN GTSNFMMTKM SEEGWTYDES 

       190        200        210        220        230        240 
LAKAQELGYA ESDPTNDVDG IDASYKLAIL SEFAFGMTLA PDDIAKSGLR SIQKTDVEIA 

       250        260        270        280        290        300 
QQFGYVLKLT GEINEVDSGI FAEVSPTFLP KSHPLASVNG VMNAVFIESE GIGDSVFYGA 

       310        320        330        340        350        360 
GAGQKPTATS VLADIVRIVK RVKDGTIGKS FNEYARSTSL ANPHDIENKY YFSVETPDST 

       370        380        390        400        410        420 
GQLLLLVELF TSENVSFEQV LQQKGNGKRA VVVIISHKIN RVQLSAIQDK LNQEKDFKLL 


NRFKVLGD

P52985 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