Reviewed, UniProtKB/Swiss-Prot P63629 (DHOM_MYCTU)

Names and origin

Protein names

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

Gene names

Name:	hom
Synonyms:	thrA
Ordered Locus Names:	Rv1294, MT1333
ORF Names:	MTCY373.14

Organism

Mycobacterium tuberculosis [Complete proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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. 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
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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NADP or NADPH 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 – 441	441	Homoserine dehydrogenase		PRO_0000066702
Regions
	Domain	355 – 433	79	ACT
	Nucleotide binding	13 – 20	8	NADP By similarity
Sites
	Active site	207	1	Proton donor Potential
	Binding site	107	1	NADP By similarity
	Binding site	192	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P63629-1 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 818248C137885BE8	FASTA	441	45,553
	10 20 30 40 50 60 MPGDEKPVGV AVLGLGNVGS EVVRIIENSA EDLAARVGAP LVLRGIGVRR VTTDRGVPIE 70 80 90 100 110 120 LLTDDIEELV AREDVDIVVE VMGPVEPSRK AILGALERGK SVVTANKALL ATSTGELAQA 130 140 150 160 170 180 AESAHVDLYF EAAVAGAIPV IRPLTQSLAG DTVLRVAGIV NGTTNYILSA MDSTGADYAS 190 200 210 220 230 240 ALADASALGY AEADPTADVE GYDAAAKAAI LASIAFHTRV TADDVYREGI TKVTPADFGS 250 260 270 280 290 300 AHALGCTIKL LSICERITTD EGSQRVSARV YPALVPLSHP LAAVNGAFNA VVVEAEAAGR 310 320 330 340 350 360 LMFYGQGAGG APTASAVTGD LVMAARNRVL GSRGPRESKY AQLPVAPMGF IETRYYVSMN 370 380 390 400 410 420 VADKPGVLSA VAAEFAKREV SIAEVRQEGV VDEGGRRVGA RIVVVTHLAT DAALSETVDA 430 440 LDDLDVVQGV SSVIRLEGTG L

References

[1]

"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.

[2]

"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX842576 Genomic DNA. Translation: CAA97759.1. AE000516 Genomic DNA. Translation: AAK45595.1.
PIR	B70773.
RefSeq	NP_215810.1. NP_335781.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	886962. 924737.
GenomeReviews	Gene locus MT1333 in contig AE000516_GR. Gene locus Rv1294 in contig AL123456_GR.
KEGG	mtc:MT1333. mtu:Rv1294.
TIGR	MT1333.
Organism-specific databases
TubercuList	Rv1294.
Phylogenomic databases
HOGENOM	P63629.
OMA	P63629. LGIVNGT.
Enzyme and pathway databases
BRENDA	1.1.1.3. 809.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR005106. Asp/hSer_DH_NAD-bd. IPR016204. Homoserine_dehydrogenase. IPR001342. Homoserine_dehydrogenase_cat. IPR019811. Homoserine_dehydrogenase_CS. [Graphical view]
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_MYCTU

Accession

Primary (citable) accession number: P63629
Secondary accession number(s): Q10601

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	June 16, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)