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Protein

Homoserine dehydrogenase

Gene

hom

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.1 Publication

Enzyme regulationi

Feedback inhibition by threonine.1 Publication

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 3 of the subpathway that synthesizes L-homoserine from L-aspartate.1 Publication
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Aspartokinase 3 (yclM), Aspartokinase 2 (lysC), Aspartokinase 1 (dapG)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Homoserine dehydrogenase (hom)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Pathwayi: L-threonine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-threonine from L-aspartate.1 Publication
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Aspartokinase 3 (yclM), Aspartokinase 2 (lysC), Aspartokinase 1 (dapG)
  2. Aspartate-semialdehyde dehydrogenase (asd)
  3. Homoserine dehydrogenase (hom)
  4. Homoserine kinase (thrB)
  5. Threonine synthase (thrC)
This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051NADPBy similarity
Binding sitei190 – 1901SubstrateBy similarity
Active sitei205 – 2051Proton donorSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 168NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Amino-acid biosynthesis, Branched-chain amino acid biosynthesis, Isoleucine biosynthesis, Methionine biosynthesis, Threonine biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBSUB:BSU32260-MONOMER.
UniPathwayiUPA00050; UER00063.
UPA00051; UER00465.

Names & Taxonomyi

Protein namesi
Recommended name:
Homoserine dehydrogenase (EC:1.1.1.3)
Short name:
HDH
Gene namesi
Name:hom
Synonyms:tdm
Ordered Locus Names:BSU32260
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433Homoserine dehydrogenasePRO_0000066692Add
BLAST

Proteomic databases

PaxDbiP19582.

Interactioni

Protein-protein interaction databases

IntActiP19582. 4 interactions.
STRINGi224308.Bsubs1_010100017506.

Structurei

3D structure databases

ProteinModelPortaliP19582.
SMRiP19582. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini350 – 42677ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the homoserine dehydrogenase family.Curated
Contains 1 ACT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105D6E. Bacteria.
COG0460. LUCA.
HOGENOMiHOG000076615.
InParanoidiP19582.
KOiK00003.
OMAiEWIAGII.
OrthoDBiEOG6XM7CQ.
PhylomeDBiP19582.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002912. ACT_dom.
IPR005106. Asp/hSer_DH_NAD-bd.
IPR016204. HDH.
IPR001342. HDH_cat.
IPR019811. HDH_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000098. Homoser_dehydrog. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19582-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKAIRVGLLG LGTVGSGVVK IIQDHQDKLM HQVGCPVTIK KVLVKDLEKK
60 70 80 90 100
REVDLPKEVL TTEVYDVIDD PDVDVVIEVI GGVEQTKQYL VDALRSKKHV
110 120 130 140 150
VTANKDLMAV YGSELLAEAK ENGCDIYFEA SVAGGIPILR TLEEGLSSDR
160 170 180 190 200
ITKMMGIVNG TTNFILTKMI KEKSPYEEVL KEAQDLGFAE ADPTSDVEGL
210 220 230 240 250
DAARKMAILA RLGFSMNVDL EDVKVKGISQ ITDEDISFSK RLGYTMKLIG
260 270 280 290 300
IAQRDGSKIE VSVQPTLLPD HHPLSAVHNE FNAVYVYGEA VGETMFYGPG
310 320 330 340 350
AGSMPTATSV VSDLVAVMKN MRLGVTGNSF VGPQYEKNMK SPSDIYAQQF
360 370 380 390 400
LRIHVKDEVG SFSKITSVFS ERGVSFEKIL QLPIKGHDEL AEIVIVTHHT
410 420 430
SEADFSDILQ NLNDLEVVQE VKSTYRVEGN GWS
Length:433
Mass (Da):47,494
Last modified:May 30, 2000 - v2
Checksum:i03E9DF7727D62696
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti375 – 3751S → T in CAA28269 (PubMed:3098560).Curated
Sequence conflicti402 – 4021E → Q in AAA50609 (PubMed:3139660).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23217 Genomic DNA. Translation: AAA50609.1.
AL009126 Genomic DNA. Translation: CAB15216.1.
X04603 Genomic DNA. Translation: CAA28269.1.
PIRiA31973. DEECHS.
RefSeqiNP_391106.1. NC_000964.3.
WP_003228694.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15216; CAB15216; BSU32260.
GeneIDi936654.
KEGGibsu:BSU32260.
PATRICi18978424. VBIBacSub10457_3375.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23217 Genomic DNA. Translation: AAA50609.1.
AL009126 Genomic DNA. Translation: CAB15216.1.
X04603 Genomic DNA. Translation: CAA28269.1.
PIRiA31973. DEECHS.
RefSeqiNP_391106.1. NC_000964.3.
WP_003228694.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliP19582.
SMRiP19582. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP19582. 4 interactions.
STRINGi224308.Bsubs1_010100017506.

Proteomic databases

PaxDbiP19582.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15216; CAB15216; BSU32260.
GeneIDi936654.
KEGGibsu:BSU32260.
PATRICi18978424. VBIBacSub10457_3375.

Phylogenomic databases

eggNOGiENOG4105D6E. Bacteria.
COG0460. LUCA.
HOGENOMiHOG000076615.
InParanoidiP19582.
KOiK00003.
OMAiEWIAGII.
OrthoDBiEOG6XM7CQ.
PhylomeDBiP19582.

Enzyme and pathway databases

UniPathwayiUPA00050; UER00063.
UPA00051; UER00465.
BioCyciBSUB:BSU32260-MONOMER.

Miscellaneous databases

PROiP19582.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002912. ACT_dom.
IPR005106. Asp/hSer_DH_NAD-bd.
IPR016204. HDH.
IPR001342. HDH_cat.
IPR019811. HDH_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000098. Homoser_dehydrog. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ENZYME REGULATION, PATHWAY.
    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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 353-433.
    Strain: 168.

Entry informationi

Entry nameiDHOM_BACSU
AccessioniPrimary (citable) accession number: P19582
Secondary accession number(s): O32122, P70991
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: May 30, 2000
Last modified: February 17, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.