ID G4R9R6_PELHB Unreviewed; 400 AA.
AC G4R9R6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 OrderedLocusNames=KKY_1453 {ECO:0000313|EMBL:AEQ51473.1};
OS Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS B2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Devosiaceae; Pelagibacterium.
OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ51473.1, ECO:0000313|Proteomes:UP000008850};
RN [1] {ECO:0000313|EMBL:AEQ51473.1, ECO:0000313|Proteomes:UP000008850}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2
RC {ECO:0000313|Proteomes:UP000008850};
RX PubMed=22156395; DOI=10.1128/JB.06343-11;
RA Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL J. Bacteriol. 194:197-198(2012).
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}.
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DR EMBL; CP003075; AEQ51473.1; -; Genomic_DNA.
DR RefSeq; WP_014130622.1; NC_016078.1.
DR AlphaFoldDB; G4R9R6; -.
DR STRING; 1082931.KKY_1453; -.
DR KEGG; phl:KKY_1453; -.
DR PATRIC; fig|1082931.4.peg.1430; -.
DR eggNOG; COG4992; Bacteria.
DR HOGENOM; CLU_016922_10_3_5; -.
DR UniPathway; UPA00098; UER00358.
DR Proteomes; UP000008850; Chromosome.
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:AEQ51473.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000008850};
KW Transferase {ECO:0000313|EMBL:AEQ51473.1}.
SQ SEQUENCE 400 AA; 42825 MW; AFDDD4378327112B CRC64;
MALTEDLIAL EQTLGAHNYK PLDVALVRGE GVFVYDVDGK QYLDCLSAYS AVNQGHCHPK
ILQAMVEQAK KLTLTSRAFH NDQLALFYQE IADLTGSHKV LPMNTGAEAV ESAIKAVRKW
GYEVKGVEKD KAEIIVCANN FHGRTMGIVG FSTDPDARGG FGPFAPGFRI IPFGDADALE
KAITPNTVGF LVEPIQGEAG VIIPPEGYFR RVRQLCTDNN VTLILDEIQT GLGRTGKLLA
EQHEGIEADV TLLGKALSGG FYPVSAVLSN SEVLGVLQPG QHGSTFGGNP LACAVARAAL
RVLTEEGMIE NAAALGPYFL EGLAGIKSNH IRSVRGRGLM LAVDLHPEAG GARKFCHTLK
EHGILAKDTH TDTIRIAPPL VITKKQIDDA LEVFGKVLAG
//
