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Q5HHC8 (OAT2_STAAC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:SACOL0960
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of ornithine to glutamate semialdehyde By similarity. HAMAP MF_01689

Catalytic activity

L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid. HAMAP MF_01689

Cofactor

Pyridoxal phosphate By similarity. HAMAP MF_01689

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1. HAMAP MF_01689

Subcellular location

Cytoplasm By similarity HAMAP MF_01689.

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. OAT subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine metabolic process

Inferred from electronic annotation. Source: InterPro

proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionornithine-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Ornithine aminotransferase 2 HAMAP MF_01689
PRO_0000112781

Amino acid modifications

Modified residue2551N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HHC8 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 37CCCCDC9840CCF3

FASTA39643,418
        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 

« Hide

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. expand/collapse author list , 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: COL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000046 Genomic DNA. Translation: AAW37928.1.
RefSeqYP_185829.1. NC_002951.2.

3D structure databases

ProteinModelPortalQ5HHC8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HHC8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000010935; EBSTAP00000010670; EBSTAG00000010934.
GeneID3237697.
GenomeReviewsGene locus SACOL0960 in contig CP000046_GR.
KEGGsac:SACOL0960.
PATRIC19528160. VBIStaAur112458_0935.
TIGRSACOL0960.

Phylogenomic databases

eggNOGCOG4992.
GeneTreeEBGT00050000024123.
HOGENOMHBG725944.
OMARSNIVRD.
PhylomeDBQ5HHC8.
ProtClustDBPRK04073.

Enzyme and pathway databases

BioCycSAUR93062:SACOL0960-MONOMER.

Family and domain databases

HAMAPMF_01689. Ornith_aminotrans_3.
[Tree]
InterProIPR004636. AcOrn/SuccinylOrn_aminoTrfase.
IPR005814. Aminotrans_3.
IPR010164. Orn_aminotrans.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
Gene3DG3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KOK00819.
PANTHERPTHR11986. Aminotrans_3. 1 hit.
PTHR11986:SF18. Orn_aminotrans. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
SUPFAMSSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
TIGRFAMsTIGR01885. Orn_aminotrans. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOAT2_STAAC
AccessionPrimary (citable) accession number: Q5HHC8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families