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Reviewed, UniProtKB/Swiss-Prot P19582 (DHOM_BACSU)

Last modified July 22, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Homoserine dehydrogenase
      Short name=HDH
    EC=1.1.1.3
Gene names
Name: hom
Synonyms: tdm
Ordered Locus Names: BSU32260
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length433 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Ontologies

Keywords

   Biological processAmino-acid biosynthesis
Branched-chain amino acid biosynthesis
Isoleucine biosynthesis
Methionine biosynthesis
Threonine biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

None. [Check GOA]

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 433433Homoserine dehydrogenase

Regions

Domain349 – 42476ACT
Nucleotide binding9 – 168NADP By similarity

Sites

Active site2051Proton donor Potential
Binding site1051NADP By similarity
Binding site1901Substrate By similarity

Experimental info

Sequence conflict3751S → T in CAA28269. Ref.3
Sequence conflict4021E → Q in AAA50609. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P19582-1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 03E9DF7727D62696

FASTA43347,494
        10         20         30         40         50         60 
MKAIRVGLLG LGTVGSGVVK IIQDHQDKLM HQVGCPVTIK KVLVKDLEKK REVDLPKEVL 

        70         80         90        100        110        120 
TTEVYDVIDD PDVDVVIEVI GGVEQTKQYL VDALRSKKHV VTANKDLMAV YGSELLAEAK 

       130        140        150        160        170        180 
ENGCDIYFEA SVAGGIPILR TLEEGLSSDR ITKMMGIVNG TTNFILTKMI KEKSPYEEVL 

       190        200        210        220        230        240 
KEAQDLGFAE ADPTSDVEGL DAARKMAILA RLGFSMNVDL EDVKVKGISQ ITDEDISFSK 

       250        260        270        280        290        300 
RLGYTMKLIG IAQRDGSKIE VSVQPTLLPD HHPLSAVHNE FNAVYVYGEA VGETMFYGPG 

       310        320        330        340        350        360 
AGSMPTATSV VSDLVAVMKN MRLGVTGNSF VGPQYEKNMK SPSDIYAQQF LRIHVKDEVG 

       370        380        390        400        410        420 
SFSKITSVFS ERGVSFEKIL QLPIKGHDEL AEIVIVTHHT SEADFSDILQ NLNDLEVVQE 

       430 
VKSTYRVEGN GWS

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References

« Hide 'large scale' references
[1]"Cloning and nucleotide sequence of the Bacillus subtilis hom gene coding for homoserine dehydrogenase. Structural and evolutionary relationships with Escherichia coli aspartokinases-homoserine dehydrogenases I and II."
Parsot C., Cohen G.N.
J. Biol. Chem. 263:14654-14660(1988) [PubMed: 3139660] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Evolution of biosynthetic pathways: a common ancestor for threonine synthase, threonine dehydratase and D-serine dehydratase."
Parsot C.
EMBO J. 5:3013-3019(1986) [PubMed: 3098560] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 353-433.
Strain: 168.

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Cross-references

Sequence databases

M23217 Genomic DNA. Translation: AAA50609.1.
Z99120 Genomic DNA. Translation: CAB15216.1.
X04603 Genomic DNA. Translation: CAA28269.1.
PIRDEECHS. A31973.
RefSeqNP_391106.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID936654.
GenomeReviewsGene locus BSU32260 in contig AL009126_GR.
KEGGbsu:BSU32260.
NMPDRfig|224308.1.peg.3232.

Organism-specific databases

SubtiListBG10460. hom. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMP19582.

Enzyme and pathway databases

BioCycBSUB224308:BSU3223-MON.

Family and domain databases

InterProIPR002912. ACT_bd.
IPR005106. Asp/hSer_DHase_NAD-bd.
IPR016204. hSer_DHase.
IPR001342. hSer_DHase_cat.
[Graphical view]
PfamPF01842. ACT. 1 hit.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF000098. Homoser_dehydrog. 1 hit.
PROSITEPS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]
ProDomP19582.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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Entry information

Entry nameDHOM_BACSU
AccessionPrimary (citable) accession number: P19582
Secondary accession number(s): O32122, P70991
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 30, 2000
Last modified: July 22, 2008
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents