ID A0A2T6C906_9BACL Unreviewed; 396 AA.
AC A0A2T6C906;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|HAMAP-Rule:MF_01689};
DE Short=OAT {ECO:0000256|HAMAP-Rule:MF_01689};
DE EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924, ECO:0000256|HAMAP-Rule:MF_01689};
DE AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|ARBA:ARBA00030587, ECO:0000256|HAMAP-Rule:MF_01689};
GN Name=rocD {ECO:0000256|HAMAP-Rule:MF_01689};
GN ORFNames=C8P63_10133 {ECO:0000313|EMBL:PTX64817.1};
OS Melghirimyces profundicolus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Melghirimyces.
OX NCBI_TaxID=1242148 {ECO:0000313|EMBL:PTX64817.1, ECO:0000313|Proteomes:UP000244240};
RN [1] {ECO:0000313|EMBL:PTX64817.1, ECO:0000313|Proteomes:UP000244240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45787 {ECO:0000313|EMBL:PTX64817.1,
RC ECO:0000313|Proteomes:UP000244240};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of ornithine to glutamate
CC semialdehyde. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01689};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01689};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004998, ECO:0000256|HAMAP-Rule:MF_01689}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. OAT subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01689}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTX64817.1}.
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DR EMBL; QBKR01000001; PTX64817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6C906; -.
DR OrthoDB; 9807885at2; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000244240; Unassembled WGS sequence.
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; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01689};
KW Aminotransferase {ECO:0000256|HAMAP-Rule:MF_01689};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01689};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW Rule:MF_01689};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01689}; Reference proteome {ECO:0000313|Proteomes:UP000244240};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01689}.
FT MOD_RES 255
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01689"
SQ SEQUENCE 396 AA; 43616 MW; 8239EC11CE10506E CRC64;
MSRNKELIEI TDKYGARNYH PLPIVISKAE GVWVEDADGK RYMDMLSAYS ALNHGHRHPK
LIRALKEQAD KVTLTSRAFH NDQLGFFYEK VANITGKERV LPMNTGAEAV ETAVKAVRRW
AYDVKNVPED RAEIIACENN FHGRTMTAVS LSSEDAYKRG FGPMLPGIKI VPYGDAEALR
KAITPNTAAF LAEPIQGEAG VIVPPEGYLK EAAAICKEHQ VLFIADEIQT GFGRTGQTFA
CDWEGVKPDM YIMGKALGGG VMPISAVAAD EEILGVFDPG SHGSTFGGNP LACAVSVAAL
DVLQEENLVE RSRELGTYFM DELKKIQNPV IKEVRGKGLF IGMELFEPAR SYCEALSDAG
LLCKETHENT IRFAPPLIIT REELDWALDK IRSVLK
//
