P23247 (DHAS2_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartate-semialdehyde dehydrogenase 2
Short name=ASA dehydrogenase 2
Short name=ASADH 2
EC=1.2.1.11

Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase 2

Gene names

Name:	asd2
Synonyms:	asd
Ordered Locus Names:	VC_2107

Organism

Vibrio cholerae

Taxonomic identifier

666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	337 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.4
Catalytic activity	L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH. Ref.4
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 Probable. Ref.5
Domain	Consists of two domains, an N-terminal nucleotide-binding domain and a C-terminal dimerization domain. Ref.5
Sequence similarities	Belongs to the aspartate-semialdehyde dehydrogenase family.
Biophysicochemical properties	Kinetic parameters: KM=0.16 mM for L-aspartate 4-semialdehyde Ref.4 KM=0.36 mM for NADP+ KM=22 mM for phosphate
Sequence caution	The sequence AAF95253.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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 electronic annotation. Source: UniProtKB-KW 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
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 electronic annotation. Source: EC protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 337

337

Aspartate-semialdehyde dehydrogenase 2 HAMAP MF_02121

PRO_0000141394

Regions

Nucleotide binding

13 – 16

4

NADP By similarity

Nucleotide binding

41 – 42

2

NADP By similarity

Nucleotide binding

162 – 163

2

NADP By similarity

Sites

Active site

132

1

Acyl-thioester intermediate

Active site

245

1

Proton acceptor By similarity

Binding site

101

1

Phosphate By similarity

Binding site

159

1

Substrate By similarity

Binding site

216

1

Phosphate By similarity

Binding site

238

1

Substrate By similarity

Binding site

316

1

NADP By similarity

Natural variations

Natural variant

40

1

E → D in strain: C7258.

Experimental info

Sequence conflict

188 – 189

2

NT → QA in CAA39048. Ref.1

Secondary structure

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337

Helix Strand Turn

Details...

Beta strand

5 – 11

7

Helix

15 – 26

12

Beta strand

31 – 38

8

Turn

40 – 44

5

Beta strand

46 – 49

4

Beta strand

52 – 58

7

Helix

59 – 61

3

Helix

64 – 66

3

Beta strand

68 – 72

5

Helix

76 – 88

13

Beta strand

92 – 95

4

Turn

99 – 102

4

Turn

111 – 113

3

Helix

115 – 123

9

Beta strand

125 – 128

4

Helix

132 – 148

17

Beta strand

150 – 163

14

Turn

204 – 206

3

Helix

212 – 224

13

Beta strand

231 – 241

11

Beta strand

243 – 255

13

Helix

259 – 268

10

Beta strand

272 – 274

3

Helix

281 – 283

3

Beta strand

289 – 291

3

Beta strand

293 – 301

9

Beta strand

304 – 316

13

Helix

317 – 336

20

Sequences

	Sequence		Length	Mass (Da)
	P23247 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 143D7E55593308FD	FASTA	337	37,375
	10 20 30 40 50 60 MSQQFNVAIF GATGAVGETM LEVLQEREFP VDELFLLASE RSEGKTYRFN GKTVRVQNVE 70 80 90 100 110 120 EFDWSQVHIA LFSAGGELSA KWAPIAAEAG VVVIDNTSHF RYDYDIPLVV PEVNPEAIAE 130 140 150 160 170 180 FRNRNIIANP NCSTIQMLVA LKPIYDAVGI ERINVTTYQS VSGAGKAGID ELAGQTAKLL 190 200 210 220 230 240 NGYPAETNTF SQQIAFNCIP QIDQFMDNGY TKEEMKMVWE TQKIFNDPSI MVNPTCVRVP 250 260 270 280 290 300 VFYGHAEAVH VETRAPIDAE QVMDMLEQTD GIELFRGADF PTQVRDAGGK DHVLVGRVRN 310 320 330 DISHHSGINL WVVADNVRKG AATNAVQIAE LLVRDYF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Avest A.R., Frits R.M. Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CDV 101.
[2]	Fando R., Benitez J. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: El Tor C7258 / Serotype O1.
[3]	"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed: 10952301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1.
[4]	"Expression and purification of aspartate beta-semialdehyde dehydrogenase from infectious microorganisms." Moore R.A., Bocik W.E., Viola R.E. Protein Expr. Purif. 25:189-194(2002) [PubMed: 12071715] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1.
[5]	"The structure of a redundant enzyme: a second isoform of aspartate beta-semialdehyde dehydrogenase in Vibrio cholerae." Viola R.E., Liu X., Ohren J.F., Faehnle C.R. Acta Crystallogr. D 64:321-330(2008) [PubMed: 18323627] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH L-ASPARTATE-SEMIALDEHYDE, SUBUNIT, DOMAIN. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X55363 Genomic DNA. Translation: CAA39048.1.
Y15281 Genomic DNA. Translation: CAA75569.1.
AE003852 Genomic DNA. Translation: AAF95253.1. Different initiation.

PIR

B82118.
S14523.

RefSeq

NP_231739.1. NC_002505.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QZ9	X-ray	2.20	A/B/C	2-337	[»]
2R00	X-ray	2.03	A/B/C	2-337	[»]

ProteinModelPortal

P23247.

SMR

P23247. Positions 2-337.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2613363.

GenomeReviews

Gene locus VC_2107 in contig AE003852_GR.

KEGG

vch:VC2107.

PATRIC

20083243. VBIVibCho83274_2013.

TIGR

VC_2107.

Phylogenomic databases

HOGENOM

HBG518238.

OMA

FHGKQVE.

PhylomeDB

P23247.

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

DHAS2_VIBCH

Accession

Primary (citable) accession number: P23247
Secondary accession number(s): O34226, Q9KQ93

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 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