Reviewed, UniProtKB/Swiss-Prot Q8TUZ5 (ARGD_METKA)

Names and origin

Protein names

Recommended name:
    Acetylornithine aminotransferase
      Short name=ACOAT
    EC=2.6.1.11

Gene names

Name:	argD
Ordered Locus Names:	MK1606

Organism

Methanopyrus kandleri [Complete proteome] [HAMAP]

Taxonomic identifier

2320 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanopyri › Methanopyrales › Methanopyraceae › Methanopyrus

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate. HAMAP MF_01107
Cofactor	Binds 1 pyridoxal phosphate per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. HAMAP MF_01107
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm Probable.
Miscellaneous	May also have succinyldiaminopimelate aminotransferase activity, thus carrying out the corresponding step in lysine biosynthesis. HAMAP MF_01107
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	arginine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate binding 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 – 389	389	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112822
Regions
	Region	104 – 105	2	Pyridoxal phosphate binding By similarity
	Region	216 – 219	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	131	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	134	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	273	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	274	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	245	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8TUZ5-1 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: AD72B13CCFE962F9	FASTA	389	42,025
	10 20 30 40 50 60 MDARELIDKY HMNTYSRFPV TLVPGEGARV WDDEGNEYID LVAGIAVNVL GHCHPAVVEA 70 80 90 100 110 120 VKEQVERLIH CSNLYYNEPQ AEAARLLAEA APKDLNKVFF CNSGTESVEC AIKLARKFTG 130 140 150 160 170 180 CTKFIAFEGG FHGRTMGALS ATWKPEFREP FEPLVPEFEH VPYGDVNAVE KAIDDDTAAV 190 200 210 220 230 240 IVEPVQGEAG VRIPPEGFLR ELRELCDEHG LLLIVDEVQS GMGRTGQFFA FEHEDVLPDI 250 260 270 280 290 300 VCLAKGLGGG VPVGATIARE EVAEAFEPGD HGSTFGGNPL ACAAVCAAVS TVLEENLPEA 310 320 330 340 350 360 AERKGKLAMR ILSEAEDVVE EVRGRGLMMG VEVGDDERAK DVAREMLDRG ALVNVTSGDV 370 380 IRLVPPLVIG EDELEKALAE LADALRASG

References

[1]

"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens." Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A. Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed: 11930014] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE010450 Genomic DNA. Translation: AAM02819.1.
RefSeq	NP_614889.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	1478201.
GenomeReviews	Gene locus MK1606 in contig AE009439_GR.
KEGG	mka:MK1606.
NMPDR	fig|190192.1.peg.1602.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q8TUZ5.
OMA	Q8TUZ5. IDCVAGI.
Enzyme and pathway databases
BioCyc	MKAN190192:MK1606-MON.
BRENDA	2.6.1.11. 7577.
Family and domain databases
HAMAP	MF_01107. [Tree]
InterPro	IPR005814. Aminotrans_3. IPR004636. ArgD_aminotrans. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00707. argD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_METKA

Accession

Primary (citable) accession number: Q8TUZ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	June 1, 2002
Last modified:	June 16, 2009
This is version 49 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)