Q6GAW9 (OAT2_STAAS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ornithine aminotransferase 2
Short name=OAT 2
EC=2.6.1.13

Alternative name(s):
Ornithine--oxo-acid aminotransferase 2

Gene names

Name:	rocD2
Ordered Locus Names:	SAS0827

Organism

Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP]

Taxonomic identifier

282459 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	396 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the interconversion of ornithine to glutamate semialdehyde By similarity. HAMAP-Rule MF_01689
Catalytic activity	L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid. HAMAP-Rule MF_01689
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1. HAMAP-Rule MF_01689
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. OAT subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway arginine metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ornithine-oxo-acid transaminase 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 – 396	396	Ornithine aminotransferase 2 HAMAP-Rule MF_01689		PRO_0000112789
Amino acid modifications
	Modified residue	255	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6GAW9 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 37CCCCDC9840CCF3	FASTA	396	43,418
	10 20 30 40 50 60 MTKSEKIIEL TNHYGAHNYL PLPIVISEAE GVWVKDPEGN KYMDMLSAYS AVNQGHRHPK 70 80 90 100 110 120 IIQALKDQAD KVTLVSRAFH SDNLGEWYEK ICKLAGKDKA LPMNTGAEAV ETALKAARRW 130 140 150 160 170 180 AYDVKGIEPN KAEIIAFNGN FHGRTMAPVS LSSEAEYQRG YGPLLDGFRK VDFGDVDALK 190 200 210 220 230 240 AAINENTAAV LVEPIQGEAG INIPPEGYLK AIRELCDEHN VLFIADEIQA GLGRSGKLFA 250 260 270 280 290 300 TDWDNVKPDV YILGKALGGG VFPISVVLAD KEVLDVFTPG SHGSTFGGNP LACAASIAAL 310 320 330 340 350 360 DVIVDEDLPG RSLELGDYFK EQLKQIDHPS IKEVRGRGLF IGVELNESAR PYCEALKEEG 370 380 390 LLCKETHDTV IRFAPPLIIT KEELDLALEK IRHVFQ

References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MSSA476.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571857 Genomic DNA. Translation: CAG42602.1.
RefSeq	YP_042954.1. NC_002953.3.
3D structure databases
ProteinModelPortal	Q6GAW9.
SMR	Q6GAW9. Positions 5-395.
ModBase	Search...
Protein-protein interaction databases
STRING	282459.SAS0827.
Proteomic databases
PRIDE	Q6GAW9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2864407.
KEGG	sas:SAS0827.
PATRIC	19551084. VBIStaAur96780_0861.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4992.
HOGENOM	HOG000020206.
KO	K00819.
OMA	RSNIVRD.
ProtClustDB	PRK04073.
Enzyme and pathway databases
UniPathway	UPA00098; UER00358.
Family and domain databases
Gene3D	3.40.640.10. 1 hit. 3.90.1150.10. 2 hits.
HAMAP	MF_01689. Ornith_aminotrans_3.
InterPro	IPR005814. Aminotrans_3. IPR010164. Orn_aminotrans. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. IPR004636. Trfase_AcOrn/SuccOrn_fam. [Graphical view]
PANTHER	PTHR11986. PTHR11986. 1 hit. PTHR11986:SF18. PTHR11986:SF18. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMs	TIGR01885. Orn_aminotrans. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

OAT2_STAAS

Accession

Primary (citable) accession number: Q6GAW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program