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Q49W96 (OAT2_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:SSP1818
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [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_0000112797

Amino acid modifications

Modified residue2551N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q49W96 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 02BC20FA8B3FEE43

FASTA39643,399
        10         20         30         40         50         60 
MSRSEEIIEV TNHYGAQNYV PLPIVISEAE GVWVKDPEGN KYMDMLSAYS AVNQGHRHPK 

        70         80         90        100        110        120 
IIQALKEQAD KVTLVSRAFH SENLGEWYEK ICKLSGKAKA LPMNTGAEAV ETALKAARRW 

       130        140        150        160        170        180 
AYDVKNIQPD KAEIIAFNGN FHGRTMAPVS LSSEPEYQRG YGPLLDGFRK VDFGDIEAVK 

       190        200        210        220        230        240 
AAINENTAAI LIEPIQGEAG INVPPEGYLK QIRELCDEHN VLFIADEIQA GLGRSGKLFA 

       250        260        270        280        290        300 
TDWDNVKPDV YILGKALGGG VLPISVVLAD EEVLGVFTPG SHGSTFGGNP LACAVSNAAL 

       310        320        330        340        350        360 
DVIIDEDLPG RSLELGDYFK SELEKIDHPA IKEVRGRGLF IGIELNEAAR PFCESLKEQG 

       370        380        390 
LLCKETHDTV IRFAPPLIIS KEELDFALDK VRSVFE 

« Hide

References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed: 16135568] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008934 Genomic DNA. Translation: BAE18963.1.
RefSeqYP_301908.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ49W96.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ49W96.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000049094; EBSTAP00000047463; EBSTAG00000049091.
GeneID3616473.
GenomeReviewsGene locus SSP1818 in contig AP008934_GR.
KEGGssp:SSP1818.
NMPDRfig|342451.4.peg.1890.
PATRIC19625221. VBIStaSap90642_1814.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4992.
GeneTreeEBGT00050000024123.
HOGENOMHBG725944.
OMACHPKILE.
PhylomeDBQ49W96.
ProtClustDBPRK04073.

Enzyme and pathway databases

BioCycSSAP342451:SSP1818-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_STAS1
AccessionPrimary (citable) accession number: Q49W96
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 51 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