Reviewed, UniProtKB/Swiss-Prot Q9A652 (ARGD_CAUCR)

Names and origin

Protein names

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

Gene names

Name:	argD
Ordered Locus Names:	CC_2243

Organism

Caulobacter crescentus (Caulobacter vibrioides) [Complete proteome] [HAMAP]

Taxonomic identifier

155892 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Caulobacterales › Caulobacteraceae › Caulobacter

Protein attributes

Sequence length	405 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 – 405	405	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112737
Regions
	Region	105 – 106	2	Pyridoxal phosphate binding By similarity
	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	N(2)-acetyl-L-ornithine By similarity
	Binding site	282	1	N(2)-acetyl-L-ornithine By similarity
	Binding site	283	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	254	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9A652-1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: DBFC6633ED1D7268	FASTA	405	42,816
	10 20 30 40 50 60 MSTATSSTTS QHHIMGVYNR APLAFERGRG ARLISTEGEE YLDCVAGIAT NGLGHAHPAL 70 80 90 100 110 120 VEVLKAQAEK LWHVSNIYRI PEQEELADAL CANSFADVVF FTNSGTEAVE CALKTARKYH 130 140 150 160 170 180 SANGQPERID IYGFDGSFHG RTYAAVNASG NPSYVDGFGP RLPGYSQLTF GDHDAIKAAI 190 200 210 220 230 240 ASPTTAAIIV EPVQGEGGAR SIPTQCLVGL RQLCDEHGVL LIYDEVQCGM GRTGKLFAYE 250 260 270 280 290 300 WAEGGEPHIM AVAKALGGGF PIGACLATTE AAKGMTVAAH GSTFGGNPLA MAVGKAALEI 310 320 330 340 350 360 IKSPETLDNV KTVSGFFTQQ LNGLKDRFPD VIVDVRGKGM LIGVKLIPNN RDFMVLARDE 370 380 390 400 KLLIAGGGDN CVRLLPPLNL TIEEASEAIA KLEKACEAAR AKAAA

References

[1]

"Complete genome sequence of Caulobacter crescentus." Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T., Dodson R.J. , Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R., Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O., Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001) [PubMed: 11259647] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 19089 / CB15.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE005673 Genomic DNA. Translation: AAK24214.1.
PIR	B87527.
RefSeq	NP_421046.1.
3D structure databases
HSSP	HSSP built from PDB template 1QJ3 based on UniProtKB P12995.
ModBase	Search...
Genome annotation databases
GeneID	943170.
GenomeReviews	Gene locus CC_2243 in contig AE005673_GR.
KEGG	ccr:CC_2243.
NMPDR	fig|190650.1.peg.2226.
TIGR	CC_2243.
Phylogenomic databases
HOGENOM	Q9A652.
OMA	NIYRIPE.
Enzyme and pathway databases
BRENDA	2.6.1.11. 2191.
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_CAUCR

Accession

Primary (citable) accession number: Q9A652

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	June 1, 2001
Last modified:	November 3, 2009
This is version 61 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)