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Q4A0N2 (OAT1_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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 1

Short name=OAT 1
EC=2.6.1.13
Alternative name(s):
Ornithine--oxo-acid aminotransferase 1
Gene names
Name:rocD1
Ordered Locus Names:SSP0220
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length394 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 – 394394Ornithine aminotransferase 1 HAMAP MF_01689
PRO_0000112796

Amino acid modifications

Modified residue2521N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4A0N2 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: D4DE3FBB2D343364

FASTA39443,538
        10         20         30         40         50         60 
MLDLYEHTDK YSSKNYSPLK LALAKGRGAK VWDIEDNCYI DCISGFSVVN QGHCHPKIIK 

        70         80         90        100        110        120 
ALQEQSQRIT MVSRALYSDN LGKWEEKICK LANKENVLPM NTGTEAVETA IKMARKWGAD 

       130        140        150        160        170        180 
IKNIDESSSE IIAMNGNFHG RTLGSLSLSS QDSYKKGFGP LLNNIHYADF GDIEQLKKLI 

       190        200        210        220        230        240 
NNQTTAIILE PIQGEGGVNI PPTHFIQEVR QLCNEYNVLL IADEIQVGLG RTGKMFAMEW 

       250        260        270        280        290        300 
ENTEPDIYLL GKSLGGGLYP ISAVLANQDV MSVLTPGTHG STFGGNPLAC AVSMAALDVL 

       310        320        330        340        350        360 
NEEHLVQNAL DLGDRLLKHL QQIESELIVE VRGRGLFIGI ELNVAAQDYC EQMINKGVLC 

       370        380        390 
KETQGNIIRI APPLVIDKDE IDEVIRVITE VLEK 

« 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: BAE17365.1.
RefSeqYP_300310.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ4A0N2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4A0N2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000047176; EBSTAP00000045545; EBSTAG00000047173.
GeneID3617138.
GenomeReviewsGene locus SSP0220 in contig AP008934_GR.
KEGGssp:SSP0220.
NMPDRfig|342451.4.peg.571.
PATRIC19621929. VBIStaSap90642_0225.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4992.
GeneTreeEBGT00050000024123.
HOGENOMHBG725944.
PhylomeDBQ4A0N2.
ProtClustDBCLSK884462.

Enzyme and pathway databases

BioCycSSAP342451:SSP0220-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.
TIGRFAMsTIGR00707. ArgD. 1 hit.
TIGR01885. Orn_aminotrans. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameOAT1_STAS1
AccessionPrimary (citable) accession number: Q4A0N2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 52 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