P0A542 (DHAS_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate-semialdehyde dehydrogenase
Short name=ASA dehydrogenase
Short name=ASADH
EC=1.2.1.11

Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase

Gene names

Name:	asd
Ordered Locus Names:	Rv3708c, MT3811
ORF Names:	MTV025.056c

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. Ref.2
Catalytic activity	L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH. Ref.2 Ref.5
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. HAMAP MF_02121 Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 2/3. HAMAP MF_02121 Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 2/5. HAMAP MF_02121
Subunit structure	Homodimer. Ref.5
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=955 µM for L-aspartate 4-semialdehyde Ref.2 KM=65 µM for NADP+ KM=11.4 mM for phosphate Vmax=51.84 µmol/min/mg enzyme towards L-aspartate 4-semialdehyde Vmax=43.74 µmol/min/mg enzyme towards NADP+ Vmax=44.04 µmol/min/mg enzyme towards phosphate

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis Methionine biosynthesis Threonine biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	diaminopimelate biosynthetic process Inferred from direct assay. Source: MTBBASE growth Inferred from mutant phenotype. Source: MTBBASE isoleucine biosynthetic process Inferred from electronic annotation. Source: InterPro methionine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from electronic annotation. Source: InterPro NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: InterPro aspartate-semialdehyde dehydrogenase activity Inferred from direct assay Ref.2Ref.5. Source: MTBBASE protein homodimerization activity Inferred from physical interaction Ref.5. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 345

345

Aspartate-semialdehyde dehydrogenase HAMAP MF_02121

PRO_0000141383

Regions

Nucleotide binding

11 – 14

4

NADP By similarity

Nucleotide binding

39 – 40

2

NADP By similarity

Nucleotide binding

160 – 161

2

NADP By similarity

Sites

Active site

130

1

Acyl-thioester intermediate By similarity

Active site

256

1

Proton acceptor By similarity

Binding site

99

1

Phosphate By similarity

Binding site

157

1

Substrate By similarity

Binding site

227

1

Phosphate By similarity

Binding site

249

1

Substrate By similarity

Binding site

325

1

NADP By similarity

Secondary structure

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345

Helix Strand Turn

Details...

Helix

17 – 24

8

Beta strand

30 – 32

3

Beta strand

34 – 36

3

Beta strand

44 – 46

3

Beta strand

51 – 56

6

Turn

57 – 59

3

Beta strand

67 – 70

4

Helix

75 – 86

12

Beta strand

90 – 93

4

Turn

97 – 100

4

Turn

109 – 111

3

Helix

113 – 116

4

Helix

130 – 146

17

Beta strand

148 – 157

10

Helix

168 – 177

10

Helix

182 – 185

4

Beta strand

197 – 201

5

Helix

223 – 235

13

Beta strand

242 – 244

3

Beta strand

257 – 266

10

Helix

270 – 277

8

Helix

291 – 294

4

Beta strand

318 – 322

5

Helix

331 – 341

11

Sequences

	Sequence		Length	Mass (Da)
	P0A542 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: C886DDB63D03E25D	FASTA	345	36,230
	10 20 30 40 50 60 MGLSIGIVGA TGQVGQVMRT LLDERDFPAS AVRFFASARS QGRKLAFRGQ EIEVEDAETA 70 80 90 100 110 120 DPSGLDIALF SAGSAMSKVQ APRFAAAGVT VIDNSSAWRK DPDVPLVVSE VNFERDAHRR 130 140 150 160 170 180 PKGIIANPNC TTMAAMPVLK VLHDEARLVR LVVSSYQAVS GSGLAGVAEL AEQARAVIGG 190 200 210 220 230 240 AEQLVYDGGA LEFPPPNTYV APIAFNVVPL AGSLVDDGSG ETDEDQKLRF ESRKILGIPD 250 260 270 280 290 300 LLVSGTCVRV PVFTGHSLSI NAEFAQPLSP ERARELLDGA TGVQLVDVPT PLAAAGVDES 310 320 330 340 LVGRIRRDPG VPDGRGLALF VSGDNLRKGA ALNTIQIAEL LTADL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mycobacterium tuberculosis ask-alpha, ask-beta and asd genes." Gilker J.M., Jucker M.T. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and characterization of aspartate-beta-semialdehyde dehydrogenase from Mycobacterium tuberculosis H37 Rv." Shafiani S., Sharma P., Vohra R.M., Tewari R. J. Appl. Microbiol. 98:832-838(2005) [PubMed: 15752328] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS. Strain: ATCC 25618 / H37Rv.
[3]	"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.
[4]	"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.
[5]	"Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis." Vyas R., Kumar V., Panjikar S., Karthikeyan S., Kishan K.V., Tewari R., Weiss M.S. Acta Crystallogr. F 64:167-170(2008) [PubMed: 18323599] [Abstract] Cited for: CRYSTALLIZATION, CATALYTIC ACTIVITY, SUBUNIT. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U90239 Genomic DNA. Translation: AAB49996.1.
AY372113 Genomic DNA. Translation: AAQ75346.1.
BX842583 Genomic DNA. Translation: CAA18030.1.
AE000516 Genomic DNA. Translation: AAK48179.1.

PIR

E70794.

RefSeq

NP_218225.1. NC_000962.2.
NP_338365.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GUL	model	-	A	1-345	[»]
3LLG	X-ray	2.18	A	2-342	[»]

ProteinModelPortal

P0A542.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000000191; EBMYCP00000000191; EBMYCG00000000191.
EBMYCT00000072321; EBMYCP00000070380; EBMYCG00000072316.

GeneID

885118.
926449.

GenomeReviews

Gene locus MT3811 in contig AE000516_GR.
Gene locus Rv3708c in contig AL123456_GR.

KEGG

mtc:MT3811.
mtu:Rv3708c.

PATRIC

18130142. VBIMycTub22151_4163.
18156852. VBIMycTub87468_4133.

TIGR

MT3811.

Organism-specific databases

TubercuList

Rv3708c.

Phylogenomic databases

GeneTree

EBGT00050000017367.

HOGENOM

HBG518238.

OMA

LELWLCG.

PhylomeDB

P0A542.

ProtClustDB

PRK14874.

Family and domain databases

HAMAP

MF_02121. ASADH.
[Tree]

InterPro

IPR000319. Asp-semialdehyde_DH_CS.
IPR012080. Asp_semialdehyde_DH.
IPR005986. Asp_semialdehyde_DH_beta.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
IPR012280. Semialdhyde_DH_dimer_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

KO

K00133.

Pfam

PF01118. Semialdhyde_dh. 1 hit.
PF02774. Semialdhyde_dhC. 1 hit.
[Graphical view]

PIRSF

PIRSF000148. ASA_dh. 1 hit.

SMART

SM00859. Semialdhyde_dh. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01296. Asd_B. 1 hit.

PROSITE

PS01103. ASD. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

DHAS_MYCTU

Accession

Primary (citable) accession number: P0A542
Secondary accession number(s): P47730, P97049, Q597F4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program