Q5HP24 (ARGD_STAEQ) 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:	SERP1089

Organism

Staphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]

Taxonomic identifier

176279 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	375 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: 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 – 375	375	Acetylornithine aminotransferase HAMAP MF_01107		PRO_0000112795
Regions
	Region	93 – 94	2	Pyridoxal phosphate binding By similarity
	Region	205 – 208	4	Pyridoxal phosphate binding By similarity
Sites
	Binding site	120	1	Pyridoxal phosphate; via carbonyl oxygen By similarity
	Binding site	123	1	N2-acetyl-L-ornithine By similarity
	Binding site	262	1	N2-acetyl-L-ornithine By similarity
	Binding site	263	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	234	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HP24 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: C974D7E547C77D3C	FASTA	375	41,314
	10 20 30 40 50 60 MSYLFNNYKR DNIEFVDANQ NELIDKDNNV YLDFSSGIGV TNLGFNMEIY QAVYNQLNLI 70 80 90 100 110 120 WHSPNLYLSS IQEEVAQKLI GQRDYLAFFC NSGTEANEAA IKLARKATGK SEIIAFKKSF 130 140 150 160 170 180 HGRTYGAMSA TGQKKITDQF GPVVPGFKFA IFNDFNSFKS LTSNNTAAVI IEIIQGESGV 190 200 210 220 230 240 LPADSLFMKQ LNEYCKQKDI LIIVDEVQTG IGRTGKLYAH EHYQLSPDII TLAKGLGNGL 250 260 270 280 290 300 PIGAMLGKKN LGHAFGYGSH GTTFGGNRLS LAAANQTLSI INDADLLNDV QSKGQFLIEN 310 320 330 340 350 360 LRKSLVNKRN VIEVRGVGLM VGIEVTNDPS QVVREAKRMG LIILTAGKNV IRLLPPLTIT 370 KKQLEKGIEI LTEII

References

[1]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000029 Genomic DNA. Translation: AAW54473.1.
RefSeq	YP_188666.1. NC_002976.3.
3D structure databases
ProteinModelPortal	Q5HP24.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HP24.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000043107; EBSTAP00000041650; EBSTAG00000043105.
GeneID	3242103.
GenomeReviews	Gene locus SERP1089 in contig CP000029_GR.
KEGG	ser:SERP1089.
NMPDR	fig|176279.3.peg.1200.
PATRIC	19613035. VBIStaEpi130894_1060.
TIGR	SERP1089.
Phylogenomic databases
eggNOG	COG4992.
GeneTree	EBGT00050000024123.
HOGENOM	HBG725944.
OMA	ANQNELI.
ProtClustDB	PRK04260.
Enzyme and pathway databases
BioCyc	SEPI176279:SERP1089-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. 1 hit.
KO	K00818.
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_STAEQ

Accession

Primary (citable) accession number: Q5HP24

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	February 15, 2005
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program