Q57843 (ADHS_METJA) Reviewed, UniProtKB/Swiss-Prot

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=2.2.1.10

Alternative name(s):
Transaldolase-like ADHS

Gene names

Ordered Locus Names:

MJ0400

Organism

Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]

Taxonomic identifier

243232 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus › Methanocaldococcus jannaschii

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). Plays 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 4-semialdehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate = 2-amino-2,3,7-trideoxy-D-lyxo-hept-6-ulosonate + 2,3-dioxopropylaldehyde phosphate. Ref.3
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) Ref.3 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	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	hydro-lyase activity Inferred from electronic annotation. Source: InterPro transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
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

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273

Helix Strand Turn

Details...

Turn

3 – 6

4

Helix

10 – 16

7

Turn

17 – 19

3

Turn

22 – 24

3

Beta strand

27 – 31

5

Helix

34 – 38

5

Beta strand

44 – 46

3

Helix

47 – 57

11

Beta strand

60 – 64

5

Helix

66 – 70

5

Beta strand

75 – 77

3

Beta strand

81 – 85

5

Beta strand

93 – 95

3

Helix

105 – 110

6

Beta strand

114 – 122

9

Helix

127 – 144

18

Beta strand

148 – 154

7

Helix

165 – 177

13

Beta strand

181 – 185

5

Helix

191 – 200

10

Beta strand

205 – 208

4

Helix

216 – 229

14

Beta strand

232 – 235

4

Helix

238 – 241

4

Beta strand

243 – 245

3

Helix

246 – 259

14

Helix

263 – 267

5

Sequences

	Sequence		Length	Mass (Da)
	Q57843 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: FUNCTION AS A FBP ALDOLASE, CATALYTIC ACTIVITY, 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] [Europe PMC] [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. NC_000909.1.

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	[»]

ProteinModelPortal

Q57843.

SMR

Q57843. Positions 1-272.

ModBase

Search...

Protein-protein interaction databases

STRING

243232.MJ0400.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAB98389; AAB98389; MJ_0400.

GeneID

1451260.

KEGG

mja:MJ_0400.

Phylogenomic databases

eggNOG

COG1830.

KO

K16306.

OMA

CEYWGMP.

ProtClustDB

PRK07226.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-14592.

SABIO-RK

Q57843.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR010210. ADH_synthase.
IPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]

Pfam

PF01791. DeoC. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01949. AroFGH_arch. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q57843.

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:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program