OAT1_STAAM
ID OAT1_STAAM Reviewed; 394 AA.
AC P60295; Q99X36;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Ornithine aminotransferase 1 {ECO:0000255|HAMAP-Rule:MF_01689};
DE Short=OAT 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01689};
GN Name=rocD1 {ECO:0000255|HAMAP-Rule:MF_01689}; OrderedLocusNames=SAV0185;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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; BA000017; BAB56347.1; -; Genomic_DNA.
DR RefSeq; WP_001084442.1; NC_002758.2.
DR AlphaFoldDB; P60295; -.
DR SMR; P60295; -.
DR PaxDb; P60295; -.
DR EnsemblBacteria; BAB56347; BAB56347; SAV0185.
DR KEGG; sav:SAV0185; -.
DR HOGENOM; CLU_016922_10_1_9; -.
DR OMA; PFMVPTY; -.
DR PhylomeDB; P60295; -.
DR BioCyc; SAUR158878:SAV_RS01070-MON; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000002481; 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:0006526; P:arginine biosynthetic process; IEA:UniProt.
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; IPR004636; AcOrn/SuccOrn_fam.
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; TIGR00707; argD; 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; Transferase.
FT CHAIN 1..394
FT /note="Ornithine aminotransferase 1"
FT /id="PRO_0000112782"
FT MOD_RES 252
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01689"
SQ SEQUENCE 394 AA; 43057 MW; D74BFF1F623D9396 CRC64;
MNSIIELTDY YSSNNYAPLK LVISKGKGVK VWDTDGKQYI DCISGFSVAN QGHCHPTIVK
AMTEQASKLS IISRVLYSDN LGKWEEKICH LAKKDKVLSL NSGTEAVEAA IKIARKWGSE
VKGITDGQVE IIAMNNNFHG RTLGSLSLSN HDAYKAGFHP LLQGTTTVDF GDIEQLTQAI
SPNTAAIILE PIQGEGGVNI PPKGYIQAVR QLCDKHQILM IADEIQVGLG RTGKWFAMEW
EQVVPDIYIL GKALGGGLYP VSAVLANNDV MRVLTPGTHG STFGGNPLAI AISTAALDVL
KDEQLVERSE RLGSFLLKAL LQLKHPSIKE IRGRGLFIGI ELNTDAAPFV DQLIQRGILC
KDTHRTIIRL SPPLVIDKEE IHQIVAAFQD VFKN