Reviewed, UniProtKB/Swiss-Prot Q7V0G0 (ARGD_PROMP)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	PMM1301

Organism

Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]

Taxonomic identifier

59919 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

Protein attributes

Sequence length	415 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 – 415	415	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112767
Regions
	Region	239 – 242	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	148	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	151	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	295	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	296	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	268	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7V0G0-1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: C1A8F4CE57A81C9E	FASTA	415	45,640
	10 20 30 40 50 60 MVDAPHSKCG TFGYVGSSPT APTLMNTYTR FDISFKKGNG CWLWDEKGKK YLDAVAGIAT 70 80 90 100 110 120 CSLGHSNRIL RKKLSAQLKK VQHISNLYKI EEQEELSKYL TKQSCAESVF FCNSGAEANE 130 140 150 160 170 180 SAIKLIKKYG NTVHKGKESF ILAAESSFHG RTLATLSATG QPKYQKGFEP MVKGFKFFKY 190 200 210 220 230 240 NDIASVKKLF EELKANNQKA SGILVEPIQG EGGVIPGDKK FFKELREICN KYNSLLILDE 250 260 270 280 290 300 VQSGVGRTGK MWGYENLEIE PDGFTLAKGL GGGHAIGALL VQKKANIFTP GDHASTFGGN 310 320 330 340 350 360 PFACRAAITV LEEIKRRKIL KNVLERGNQL NEGFTKISAK FPKIISGIRG LGLIQGLVIN 370 380 390 400 410 DSYTDAKTIT LKAFDKGLLL VPAGGNVVRF VPPLIISRNE INILLKKLDL IFEEM

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
EMBLGenBankDDBJ	BX548174 Genomic DNA. Translation: CAE19760.1. Different initiation.
RefSeq	NP_893418.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q7V0G0.
Genome annotation databases
GeneID	1726200.
GenomeReviews	Gene locus PMM1301 in contig BX548174_GR.
KEGG	pmm:PMM1301.
NMPDR	fig|59919.1.peg.1297.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7V0G0.
OMA	IQGLVIN.
Enzyme and pathway databases
BioCyc	PMAR167540:PMM1301-MON.
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_PROMP

Accession

Primary (citable) accession number: Q7V0G0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 5, 2009
Last modified:	November 3, 2009
This is version 49 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)