Reviewed, UniProtKB/Swiss-Prot Q7V8L1 (ARGD_PROMM)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	PMT_0331

Organism

Prochlorococcus marinus (strain MIT 9313) [Complete proteome] [HAMAP]

Taxonomic identifier

74547 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	418 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 – 418	418	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112766
Regions
	Region	240 – 243	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	149	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	152	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	296	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	297	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	269	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7V8L1-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: BBFC5EE4E6FF41B1	FASTA	418	45,677
	10 20 30 40 50 60 MVDALDSKSS AFGHVGSSPT APTAVMGTYK RFPVTLLRGK GCWVWDDHGH QYLDAVAGIA 70 80 90 100 110 120 TCALGHSDRA LRRSLGQQLK QLQHVSNLYR IPEQEALAHW LVENSCADSV FFCNSGAEAN 130 140 150 160 170 180 EAAIKLARKH GHRRRGIDRP IILTANSSFH GRTLAAISAT GQPNFHKGFE PMVEGFEFFP 190 200 210 220 230 240 FNNLQAFEQQ LNRLEAQGPS VAAVLIEPLQ GEGGVNPGEA GFFRRLRELC SQHQILLIFD 250 260 270 280 290 300 EVQVGMGRCG NWWGYQQLGI EPDAFTLAKG LGGGHAIGAL LVKQHADLFE PGDHASTFGG 310 320 330 340 350 360 NPFACKAALT VAKEIERRGL IAKVQQRGAQ LREGLTDLVQ RFPRQLKGVR GWGLLQGLVL 370 380 390 400 410 QDESTFTAPN VAQAALEEKL LVIAAGPKVV RMVPPLIIKP SEIRQLLQRL EATLAHFR

References

[1]

"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation." Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W. Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX548175 Genomic DNA. Translation: CAE20506.1.
RefSeq	NP_894164.1.
3D structure databases
SMR	Q7V8L1. Positions 25-415.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7V8L1.
Genome annotation databases
GeneID	1729610.
GenomeReviews	Gene locus PMT_0331 in contig BX548175_GR.
KEGG	pmt:PMT0331.
NMPDR	fig|74547.1.peg.331.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4992.
HOGENOM	HBG725944.
OMA	VALVFRQ.
Enzyme and pathway databases
BioCyc	PMAR74547:PMT0331-MONOMER.
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_PROMM

Accession

Primary (citable) accession number: Q7V8L1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 52 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)