PDBsum entry: 1vef

Transferase

PDB id

1vef

Contents

			Protein chains

					387 a.a. *

			Ligands

					PLP ×2

			Waters ×383

* Residue conservation analysis

PDB id:

1vef

Links
- PDBe
- RCSB
- SRS
- MMDB
- JenaLib
- OCA
- PDBWiki
- Proteopedia
- CATH
- SCOP
- FSSP
- HSSP
- PDBSWS
- PQS
- CSA
- PROCOGNATE
- ProSAT
- EDS
- Whatcheck

Name:

Transferase

Title:

Acetylornithine aminotransferase from thermus thermophilus h

Structure:

Acetylornithine/acetyl-lysine aminotransferase. Chain: a, b. Synonym: acetylornithine aminotransferase. Engineered: yes

Source:

Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.35Å

R-factor:

0.195

R-free:

0.209

Authors:

M.Matsumura,M.Goto,R.Omi,I.Miyahara,K.Hirotsu,Riken Structur Genomics/proteomics Initiative (Rsgi)

Key ref:

M.Matsumura et al. Three-Dimensional strutcure of acetylornithine aminotransferase from thermus thermophilus hb8. To be published,

Date:

30-Mar-04

Release date:

02-Aug-05

PROCHECK

	Headers

	References

Protein chains

Q93R93 (ARGD_THET2) - Acetylornithine/acetyl-lysine aminotransferase

Seq: Struc:					395 a.a. 387 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

E.C.2.6.1.11 - Acetylornithine transaminase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Pathway:

Ornithine Biosynthesis

Reaction:

N₂-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate

N(2)-acetyl-L-ornithine	+	2-oxoglutarate	=	N-acetyl-L-glutamate 5-semialdehyde	+	L-glutamate

Cofactor:

Pyridoxal 5'-phosphate

Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) matches with 93.75% similarity

Molecule diagrams generated from .mol files obtained from the KEGG ftp site



		Gene Ontology (GO) functional annotation

Cellular component	cytoplasm	1 term
Biological process	cellular amino acid biosynthetic process	4 terms
Biochemical function	catalytic activity	5 terms