ID OAT2_STAAR Reviewed; 396 AA.
AC Q6GID1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Ornithine aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01689};
DE Short=OAT 2 {ECO:0000255|HAMAP-Rule:MF_01689};
DE EC=2.6.1.13 {ECO:0000255|HAMAP-Rule:MF_01689};
DE AltName: Full=Ornithine--oxo-acid aminotransferase 2 {ECO:0000255|HAMAP-Rule:MF_01689};
GN Name=rocD2 {ECO:0000255|HAMAP-Rule:MF_01689}; OrderedLocusNames=SAR0919;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Catalyzes the interconversion of ornithine to glutamate
CC semialdehyde. {ECO:0000255|HAMAP-Rule:MF_01689}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2-oxocarboxylate + L-ornithine = an L-alpha-amino acid + L-
CC glutamate 5-semialdehyde; Xref=Rhea:RHEA:13877, ChEBI:CHEBI:35179,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:58066, ChEBI:CHEBI:59869; EC=2.6.1.13;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01689};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01689};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01689}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01689}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. OAT subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01689}.
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DR EMBL; BX571856; CAG39925.1; -; Genomic_DNA.
DR RefSeq; WP_000167321.1; NC_002952.2.
DR AlphaFoldDB; Q6GID1; -.
DR SMR; Q6GID1; -.
DR KEGG; sar:SAR0919; -.
DR HOGENOM; CLU_016922_10_1_9; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004587; F:ornithine aminotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR HAMAP; MF_01689; Ornith_aminotrans_3; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR010164; Orn_aminotrans.
DR InterPro; IPR034757; Ornith_aminotrans_bact.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR01885; Orn_aminotrans; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF18; ORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Aminotransferase; Cytoplasm; Proline biosynthesis;
KW Pyridoxal phosphate; Transferase.
FT CHAIN 1..396
FT /note="Ornithine aminotransferase 2"
FT /id="PRO_0000112787"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
SQ SEQUENCE 396 AA; 43472 MW; 316DF664A635423F CRC64;
MTKSEKIIEL TNHYGAHNYL PLPIVISEAE GVWVKDPEGN KYMDMLSAYS AVNQGHRHPK
IIQALKDQAD KVTLVSRAFH SDNLGEWYEK ICKLAGKDKA LPMNTGAEAV ETALKAARRW
AYDVKGIEPN KAEIIAFNGN FHGRTMAPVS LSSEAEYQRG YGPLLDGFRK VDFGDVDALK
AAINKNTAAV LVEPIQGEAG INIPPEGYLK AIRELCDEHN VLFIADEIQA GLGRSGKLFA
RDWDNVKPDV YILGKALGGG VFPISVVLAD KEVLDVFTPG SHGSTFGGNP LACAASIAAL
DVIVDEDLPG RSLELGDYFK EQLKQIDHPS IKEVRGRGLF IGVELNESAR PYCEALKEEG
LLCKETHDTV IRFAPPLIIT KEELDLALEK IRHVFQ
//
