Reviewed, UniProtKB/Swiss-Prot O27392 (ARGD_METTH)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	MTH_1337

Organism

Methanobacterium thermoautotrophicum [Complete proteome] [HAMAP]

Taxonomic identifier

187420 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter

Protein attributes

Sequence length	390 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 – 390	390	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112824
Regions
	Region	217 – 220	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	132	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	135	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	274	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	275	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	246	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O27392-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 5F309E073D7DA8FC	FASTA	390	41,763
	10 20 30 40 50 60 MDSEEIIELE RKFIMQTYTR QPIVLSHGKG ATVWDIEGNS YIDCFAGVAV NSIGHAHPKV 70 80 90 100 110 120 ALAICHQAQR LIHSSNIYYT REQVELAKLL TAISPHDRVF FANSGAEANE GAIKLARKFT 130 140 150 160 170 180 GKSEIIAAEN SFHGRTLATV TATGQKKYSE PFRPLPEGFK HVPYGDIGAM ADAVGDETAA 190 200 210 220 230 240 IILEPVQGEG GVIIPPEGYL KDVQELARQN DVLLILDEVQ TGFGRTGAMF ASQLFGVEPD 250 260 270 280 290 300 ITTVAKAMGG GYPIGAVLAN ERVAMAFEPG DHGSTFGGNP WGCAAAIATI EVLMDEKLPE 310 320 330 340 350 360 RAAKMGSYFL GRLRQVLHGC DAVRDIRGVG LMIGIEIDGE CAGVVDAARE MGVLINCTAG 370 380 390 KVIRIVPPLV IKKEEIDAAV DVLGHVISDL

References

[1]

"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N. J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE000666 Genomic DNA. Translation: AAB85815.1.
PIR	G69044.
RefSeq	NP_276454.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Protein-protein interaction databases
STRING	O27392.
Genome annotation databases
GeneID	1471054.
GenomeReviews	Gene locus MTH_1337 in contig AE000666_GR.
KEGG	mth:MTH1337.
NMPDR	fig|187420.1.peg.1309.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	O27392.
OMA	IDCVAGI.
Enzyme and pathway databases
BioCyc	MTHE187420:MTH1337-MON.
BRENDA	2.6.1.11. 270.
Family and domain databases
HAMAP	MF_01107. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. 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_METTH

Accession

Primary (citable) accession number: O27392

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 73 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)