Reviewed, UniProtKB/Swiss-Prot Q8PX16 (ARGD_METMA)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	MM_1406

Organism

Methanosarcina mazei (Methanosarcina frisia) [Complete proteome] [HAMAP]

Taxonomic identifier

2209 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
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. HAMAP MF_01107
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. HAMAP MF_01107
Subcellular location	Cytoplasm Probable HAMAP MF_01107.
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 – 395	395	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112823
Regions
	Region	230 – 233	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	144	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	147	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	285	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	286	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	259	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8PX16-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 4D8FF38F72E24599	FASTA	395	42,359
	10 20 30 40 50 60 MTDKIINSGN LEAGYDSVID KDSKYVMQTY GRQPLVLSKG KGAVVQDIYG KEYIDCVAGI 70 80 90 100 110 120 AVNNVGHCHP TVVKAIQAQA EKLIHVSNLY YTEIQAEFAE TLASITGMEC VFFCNSGAEA 130 140 150 160 170 180 VEAAMKLARV ATGKSAFVAA EHSFHGRTIG ALSVTHKSMY RDPFMPPVSS KTSFVPYSDA 190 200 210 220 230 240 DAIRKAISED TAAVVLEPIQ GEGGVNVPDP GYLKEVREIC DETGTLLIFD EVQTGFGRTG 250 260 270 280 290 300 TWFCKEQFGV EPDIMSMAKA IGGGFPMGAI AARSGLSFGR GQHASTFGGG PLACAAALAS 310 320 330 340 350 360 IQAIKEEKLL ERSKEMGAYF TKKLSGMARD DIVEVRGKGL MIGVEIKYPC GKFVDFAREH 370 380 390 GVLVNCTSDS VLRLVPPLVI TKEQIDSVVD VLEQA

References

[1]

"The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. , Klenk H.-P., Gunsalus R.P., Fritz H.-J., Gottschalk G. J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11883 / OCM 88.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE008384 Genomic DNA. Translation: AAM31102.1.
RefSeq	NP_633430.1.
3D structure databases
SMR	Q8PX16. Positions 24-395.
ModBase	Search...
Genome annotation databases
GeneID	1479748.
GenomeReviews	Gene locus MM_1406 in contig AE008384_GR.
KEGG	mma:MM_1406.
NMPDR	fig|192952.1.peg.1406.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	INCTSDT.
Enzyme and pathway databases
BioCyc	MMAZ192952:MM1406-MONOMER.
BRENDA	2.6.1.11. 261165.
Family and domain databases
HAMAP	MF_01107. ArgD_aminotrans_3. [Tree]
InterPro	IPR004636. AcOrn/succinylOrn_aminoTrfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase_major_dom. 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_METMA

Accession

Primary (citable) accession number: Q8PX16

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	October 1, 2002
Last modified:	February 9, 2010
This is version 58 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)