NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
PubMed=1333566 [NCBI, ExPASy, EBI, Israel, Japan]
Clepet C., Borne F., Krishnapillai V., Baird C., Patte J.-C., Cami B.;
"Isolation, organization and expression of the Pseudomonas aeruginosa threonine genes.";
Mol. Microbiol. 6:3109-3119(1992).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
DOI=10.1038/35023079; PubMed=10984043 [NCBI, ExPASy, EBI, Israel, Japan]
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen.";
Nature 406:959-964(2000).

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 .
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.
SEQUENCE CAUTION:
- Sequence=CAA46167.1; Type=Frameshift; Positions=Several;

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

X65033; CAA46167.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE004091; AAG07123.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H83179; H83179.
S27979; DEPSHA.

RefSeq

NP_252425.1; -.

3D structure databases

ModBase

P29365.

Enzyme and pathway databases

BioCyc

PAER208964:PA3736-MON; -.

Organism-specific databases

PseudoCAP

PA3736; -.

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.

BLOCKS

P29365.

Genome annotation databases

880337; -.

AE004091_GR; PA3736.

pae:PA3736; -.

fig|208964.1.peg.3735; -.

Phylogenomic databases

HOGENOM

P29365; -.

Genome annotation databases

CMR

P29365; PA3736.

Other

ProtoNet

P29365.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 434`	`434`	`Homoserine dehydrogenase.`	`PRO_0000066703`
`DOMAIN`	`352 427`	`76`	`ACT.`
`NP_BIND`	`9 16`	`8`	`NADP (By similarity).`
`ACT_SITE`	`203 203`		`Proton donor (Potential).`
`BINDING`	`103 103`		`NADP (By similarity).`
`BINDING`	`188 188`		`Substrate (By similarity).`
`CONFLICT`	`81 85`		`YTLAH -> PPWPI (in Ref. 1; CAA46167).`
`CONFLICT`	`187 190`		`AEAD -> GRGRS (in Ref. 1; CAA46167).`
`CONFLICT`	`202 202`		`H -> T (in Ref. 1; CAA46167).`
`CONFLICT`	`210 214`		`IAFGI -> MLRH (in Ref. 1; CAA46167).`
`CONFLICT`	`276 277`		`NG -> TA (in Ref. 1; CAA46167).`
`CONFLICT`	`402 402`		`R -> H (in Ref. 1; CAA46167).`

Sequence information

Length: 434 AA [This is the length of the unprocessed precursor]

Molecular weight: 46224 Da [This is the MW of the unprocessed precursor]

CRC64: 68770627B8AD9746 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPVKVGICG LGTVGGGTFN VLERNAEEIA RRAGRGIEVA QIAARRPNPK CDTGATPITA 

        70         80         90        100        110        120 
DIFDVACNPE IDVVVELIGG YTLAHELVLK AIENGKHVVT ANKALIAVHG NEIFAKAREK 

       130        140        150        160        170        180 
GVIVAFEAAV AGGIPVIKAI REGLSANRIN WLAGIINGTG NFILSEMREK GRTFPDVLAE 

       190        200        210        220        230        240 
AQALGYAEAD PTFDVEGIDA AHKLTILASI AFGIPLQFDK AYTEGISKLT SADVNYADAL 

       250        260        270        280        290        300 
GYRIKHLGVA RRTESGFELR VHPTLIPSDR LIANVNGVMN AVMVNGDAVG STLYYGAGAG 

       310        320        330        340        350        360 
MEPTASSVVA DLVDVVRAMT SDPENRVPHL AFQPDALSDH PILPIEACES AYYLRIQAKD 

       370        380        390        400        410        420 
HPGVLAQVAT ILSERGINIE SIMQKEAEEQ DGLVPMILVT HRVIEQRIND AIAALEALEG 

       430 
VSGPVVRIRV EQLN

P29365 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