ID A0A369TD80_9PROT Unreviewed; 405 AA.
AC A0A369TD80;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=ornithine aminotransferase {ECO:0000256|ARBA:ARBA00012924};
DE EC=2.6.1.13 {ECO:0000256|ARBA:ARBA00012924};
DE AltName: Full=Ornithine--oxo-acid aminotransferase {ECO:0000256|ARBA:ARBA00030587};
GN Name=rocD {ECO:0000313|EMBL:RDD63311.1};
GN ORFNames=DRB17_02340 {ECO:0000313|EMBL:RDD63311.1};
OS Ferruginivarius sediminum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Ferruginivarius.
OX NCBI_TaxID=2661937 {ECO:0000313|EMBL:RDD63311.1, ECO:0000313|Proteomes:UP000253941};
RN [1] {ECO:0000313|EMBL:RDD63311.1, ECO:0000313|Proteomes:UP000253941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WD2A32 {ECO:0000313|EMBL:RDD63311.1,
RC ECO:0000313|Proteomes:UP000253941};
RA Wang S.;
RT "Venubactetium sediminum gen. nov., sp. nov., isolated from a marine solar
RT saltern.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-ornithine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004998}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:RDD63311.1}.
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DR EMBL; QPMH01000002; RDD63311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369TD80; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000253941; Unassembled WGS sequence.
DR GO; GO:0004587; F:ornithine aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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 InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR010164; Orn_aminotrans.
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 Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:RDD63311.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000253941};
KW Transferase {ECO:0000313|EMBL:RDD63311.1}.
SQ SEQUENCE 405 AA; 44435 MW; 86FEE0A170F12AB2 CRC64;
MREARAMNQQ DTIISLTETY SAHNYHPLPV VLTKGEGVWV WDVEGRRYLD CLSAYSALNQ
GHRHPAIIDA LTAQAGRITL TSRAFHNDRM GKFLQLLCKT AGMEMALPMN TGAEAVETAI
KAARKWGYTR KGVPQDQAEI IVCNENFHGR TTTAVSLSSD PDTRRDFGPF TPGFKWVPFG
DAAALAEAMT ENTVALILEP IQGEAGINVP PDGYLRECRR ICDRHNALFV VDEIQTGLGR
TGALFCHQHE DGADPDMMIL GKALGGGVYP VSAVVSSREI LGVFQPGDHG STFGGNPLAC
EVARASLRVI LDEGLAERSR YLGARLYERL RSLNSPRIKE VRGRGLMIGV EIDKAHGPAR
PICEALMRRG VLCKETHEQV IRLAPPLVIQ ESEIDWLGDQ MAAIL
//
