OAT2_STAS1
ID OAT2_STAS1 Reviewed; 396 AA.
AC Q49W96;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 113.
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=SSP1818;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18963.1; -; Genomic_DNA.
DR RefSeq; WP_002483795.1; NZ_MTGA01000039.1.
DR AlphaFoldDB; Q49W96; -.
DR SMR; Q49W96; -.
DR STRING; 342451.SSP1818; -.
DR EnsemblBacteria; BAE18963; BAE18963; SSP1818.
DR KEGG; ssp:SSP1818; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_1_9; -.
DR OMA; DVFPRFA; -.
DR OrthoDB; 572533at2; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000006371; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0050155; F:ornithine(lysine) transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0004587; F:ornithine-oxo-acid transaminase 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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01689; Ornith_aminotrans_3; 1.
DR InterPro; IPR005814; Aminotrans_3.
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 PANTHER; PTHR11986:SF18; PTHR11986:SF18; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01885; Orn_aminotrans; 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; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Ornithine aminotransferase 2"
FT /id="PRO_0000112797"
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
SQ SEQUENCE 396 AA; 43399 MW; 02BC20FA8B3FEE43 CRC64;
MSRSEEIIEV TNHYGAQNYV PLPIVISEAE GVWVKDPEGN KYMDMLSAYS AVNQGHRHPK
IIQALKEQAD KVTLVSRAFH SENLGEWYEK ICKLSGKAKA LPMNTGAEAV ETALKAARRW
AYDVKNIQPD KAEIIAFNGN FHGRTMAPVS LSSEPEYQRG YGPLLDGFRK VDFGDIEAVK
AAINENTAAI LIEPIQGEAG INVPPEGYLK QIRELCDEHN VLFIADEIQA GLGRSGKLFA
TDWDNVKPDV YILGKALGGG VLPISVVLAD EEVLGVFTPG SHGSTFGGNP LACAVSNAAL
DVIIDEDLPG RSLELGDYFK SELEKIDHPA IKEVRGRGLF IGIELNEAAR PFCESLKEQG
LLCKETHDTV IRFAPPLIIS KEELDFALDK VRSVFE
