Reviewed, UniProtKB/Swiss-Prot Q57843 (ADHS_METJA)

Names and origin

Protein names

Recommended name:
    2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase
      Short name=ADH synthase
      Short name=ADHS
    EC=4.1.2.n5
Alternative name(s):
    Transaldolase-like ADHS

Gene names

Ordered Locus Names:

MJ0400

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes a transaldol reaction between 6-deoxy-5-ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) with an elimination of hydroxypyruvaldehyde phosphate to yield 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH). Play a key role in an alternative pathway of the biosynthesis of 3-dehydroquinate (DHQ), which is involved in the canonical pathway for the biosynthesis of aromatic amino acids. Can also catalyze the cleavage of fructose-1,6-bisphosphate (FBP) to glyceraldehyde-3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP). Ref.2 Ref.3
Catalytic activity	L-aspartate semialdehyde + 6-deoxy-5-ketofructose 1-phosphate = hydroxypyruvaldehyde phosphate+ 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate.
Enzyme regulation	Inhibited by NaBH4 in the presence of FBP. Ref.3
Subunit structure	Homodecamer. Ref.4
Sequence similarities	Belongs to the deoC/fbaB aldolase family. ADHS subfamily.
Biophysicochemical properties	Kinetic parameters: KM=430 µM for fructose-1,6-bisphosphate (at pH 7 and 50 degrees Celsius) Vmax=33 nmol/min/mg enzyme (at pH 7 and 50 degrees Celsius) Temperature dependence: Optimum temperature is not reached at 100 degrees Celsius.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aldehyde-lyase activity Inferred from electronic annotation. Source: EC hydro-lyase 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 – 273

273

2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase

PRO_0000138957

Regions

Region

33 – 37

5

DKFP binding

Region

153 – 155

3

DKFP binding

Region

209 – 210

2

DKFP binding

Region

237 – 238

2

DKFP binding

Sites

Active site

33

1

Proton acceptor Probable

Active site

153

1

Proton donor Probable

Active site

184

1

Schiff-base intermediate with substrate

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

273

Helix Strand Turn

Details...

Turn

3 – 6

4

Helix

13 – 16

4

Turn

17 – 19

3

Turn

22 – 24

3

Beta strand

29 – 31

3

Helix

47 – 55

9

Beta strand

61 – 64

4

Beta strand

83 – 85

3

Beta strand

93 – 95

3

Helix

105 – 110

6

Beta strand

115 – 122

8

Helix

127 – 133

7

Helix

137 – 143

7

Beta strand

148 – 154

7

Helix

165 – 173

9

Beta strand

182 – 185

4

Helix

191 – 198

8

Beta strand

205 – 207

3

Helix

216 – 228

13

Turn

239 – 242

4

Beta strand

243 – 245

3

Helix

250 – 259

10

Helix

264 – 267

4

Sequences

	Sequence		Length	Mass (Da)
	Q57843-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 06DDA2E51E8275E6	FASTA	273	29,675
	10 20 30 40 50 60 MELFKDIKNL GKLVRLERIF NRESEKTVIV PMDHGVSNGP IKGLIDIRKT VNDVAEGGAN 70 80 90 100 110 120 AVLLHKGIVR HGHRGYGKDV GLIIHLSGGT AISPNPLKKV IVTTVEEAIR MGADAVSIHV 130 140 150 160 170 180 NVGSDEDWEA YRDLGMIAET CEYWGMPLIA MMYPRGKHIQ NERDPELVAH AARLGAELGA 190 200 210 220 230 240 DIVKTSYTGD IDSFRDVVKG CPAPVVVAGG PKTNTDEEFL QMIKDAMEAG AAGVAVGRNI 250 260 270 FQHDDVVGIT RAVCKIVHEN ADVEEALKEI RKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"L-aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are the precursors to the aromatic amino acids in Methanocaldococcus jannaschii." White R.H. Biochemistry 43:7618-7627(2004) [PubMed: 15182204] [Abstract] Cited for: FUNCTION AS AN ADH SYNTHASE.
[3]	"MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6-bisphosphate aldolase activity." Samland A.K., Wang M., Sprenger G.A. FEMS Microbiol. Lett. 281:36-41(2008) [PubMed: 18318840] [Abstract] Cited for: FUNCTION AS A FBP ALDOLASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[4]	"Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid synthase, a catalyst in the archaeal pathway for the biosynthesis of aromatic amino acids." Morar M., White R.H., Ealick S.E. Biochemistry 46:10562-10571(2007) [PubMed: 17713928] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, REACTION MECHANISM, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L77117 Genomic DNA. Translation: AAB98389.1.

PIR

H64349.

RefSeq

NP_247374.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2QJG	X-ray	2.60	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T	1-273	[»]
2QJH	X-ray	2.60	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T	1-273	[»]
2QJI	X-ray	2.80	A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T	1-273	[»]

ModBase

Search...

Genome annotation databases

GeneID

1451260.

GenomeReviews

Gene locus MJ0400 in contig L77117_GR.

KEGG

mja:MJ0400.

NMPDR

fig|243232.1.peg.411.

TIGR

MJ0400.

Phylogenomic databases

HOGENOM

HBG553580.

OMA

VRHGHRG.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14592.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR010210. AroFGH_arch.
IPR002915. DeoC/AroFGH_arch.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF01791. DeoC. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01949. AroFGH_arch. 1 hit.

ProtoNet

Search...

Entry information

Entry name

ADHS_METJA

Accession

Primary (citable) accession number: Q57843

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 55 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)