Q7VMS5 (ARGD_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	HD_0892

Organism

Haemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]

Taxonomic identifier

233412 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	393 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.
Sequence caution	The sequence AAP95778.1 differs from that shown. Reason: Erroneous initiation.

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: UniProtKB-KW
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: EC 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 – 393	393	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112747
Regions
	Region	224 – 227	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	138	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	141	1	N2-acetyl-L-ornithine By similarity
	Binding site	281	1	N2-acetyl-L-ornithine By similarity
	Binding site	282	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	253	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VMS5 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: 419D7208D4BA20DB	FASTA	393	42,747
	10 20 30 40 50 60 MTSDQIKQLD ANYIAQTYAK FDLALSHGQG CEVWDFDGNK YLDFTSGIGV NSLGWADPDW 70 80 90 100 110 120 LEAVIAQLHK LSHTSNLFYT EPSARLAKHL VQVSGLKRVF FANSGAEANE GAIKVARKYS 130 140 150 160 170 180 HDKYGDTRST IISLVNSFHG RTISTLAATG QKLFHQHFFP FTAGFEHLIA NDLNAFKTRI 190 200 210 220 230 240 AQNDICAIIL EVVQGEGGVC SLDQAYLQAV QGLCQVQDIL LIIDEVQTGI GRTGTMFAYQ 250 260 270 280 290 300 QFELKPDIVT LAKGLAGGLP IGAFLLADKV AETLAKGDHG STFGANPVSC AAANAVLTKL 310 320 330 340 350 360 EPLFLTEVMR KGQKLRKALQ SLPHVKSISG LGLMIGVEFD EHINVADVVT NCLKQGVLFL 370 380 390 TAKTKLRMLP PLIINDEQLE RGVTVLAQVL SEM

References

[1]

"The complete genome sequence of Haemophilus ducreyi." Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017143 Genomic DNA. Translation: AAP95778.1. Different initiation.
RefSeq	NP_873389.1. NC_002940.2.
3D structure databases
ProteinModelPortal	Q7VMS5.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1490835.
GenomeReviews	Gene locus HD_0892 in contig AE017143_GR.
KEGG	hdu:HD0892.
NMPDR	fig|233412.1.peg.754.
PATRIC	20178181. VBIHaeDuc133973_0734.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	LYEIEPD.
ProtClustDB	PRK02627.
Enzyme and pathway databases
BioCyc	HDUC233412:HD_0892-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. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K00821.
PANTHER	PTHR11986. Aminotrans_3. 1 hit. PTHR11986:SF19. ArgD_aminotrans. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR00707. ArgD. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARGD_HAEDU

Accession

Primary (citable) accession number: Q7VMS5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 5, 2009
Last modified:	January 25, 2012
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program