P19582 (DHOM_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Homoserine dehydrogenase
Short name=HDH
EC=1.1.1.3

Gene names

Name:	hom
Synonyms:	tdm
Ordered Locus Names:	BSU32260

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	433 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Isoleucine biosynthesis Methionine biosynthesis Threonine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	isoleucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP binding Inferred from electronic annotation. Source: InterPro amino acid binding Inferred from electronic annotation. Source: InterPro homoserine dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 433	433	Homoserine dehydrogenase		PRO_0000066692
Regions
	Domain	349 – 424	76	ACT
	Nucleotide binding	9 – 16	8	NADP By similarity
Sites
	Active site	205	1	Proton donor Potential
	Binding site	105	1	NADP By similarity
	Binding site	190	1	Substrate By similarity
Experimental info
	Sequence conflict	375	1	S → T in CAA28269. Ref.3
	Sequence conflict	402	1	E → Q in AAA50609. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P19582 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 03E9DF7727D62696	FASTA	433	47,494
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M23217 Genomic DNA. Translation: AAA50609.1. AL009126 Genomic DNA. Translation: CAB15216.1. X04603 Genomic DNA. Translation: CAA28269.1.
PIR	DEECHS. A31973.
RefSeq	NP_391106.1. NC_000964.3.
3D structure databases
ProteinModelPortal	P19582.
SMR	P19582. Positions 1-431.
ModBase	Search...
Protein-protein interaction databases
IntAct	P19582. 4 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000003656; EBBACP00000003656; EBBACG00000003649.
GeneID	936654.
GenomeReviews	Gene locus BSU32260 in contig AL009126_GR.
KEGG	bsu:BSU32260.
NMPDR	fig|224308.1.peg.3232.
PATRIC	18978424. VBIBacSub10457_3375.
Organism-specific databases
GenoList	BSU32260. [Micado]
Phylogenomic databases
GeneTree	EBGT00050000002519.
HOGENOM	HBG527379.
OMA	VHPAMIP.
PhylomeDB	P19582.
ProtClustDB	PRK06349.
Enzyme and pathway databases
BioCyc	BSUB:BSU32260-MONOMER.
Family and domain databases
InterPro	IPR002912. ACT-bd. IPR005106. Asp/hSer_DH_NAD-bd. IPR016204. HDH. IPR001342. HDH_cat. IPR019811. HDH_CS. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00003.
Pfam	PF01842. ACT. 1 hit. PF00742. Homoserine_dh. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view]
PIRSF	PIRSF000098. Homoser_dehydrog. 1 hit.
PROSITE	PS01042. HOMOSER_DHGENASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DHOM_BACSU

Accession

Primary (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:	January 25, 2012
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program