ID   A0A3M0CDX9_9PROT        Unreviewed;       441 AA.
AC   A0A3M0CDX9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=4-aminobutyrate aminotransferase-like enzyme {ECO:0000313|EMBL:RMB04946.1};
GN   ORFNames=BXY39_2520 {ECO:0000313|EMBL:RMB04946.1};
OS   Eilatimonas milleporae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Kordiimonadales;
OC   Kordiimonadaceae; Eilatimonas.
OX   NCBI_TaxID=911205 {ECO:0000313|EMBL:RMB04946.1, ECO:0000313|Proteomes:UP000271227};
RN   [1] {ECO:0000313|EMBL:RMB04946.1, ECO:0000313|Proteomes:UP000271227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25217 {ECO:0000313|EMBL:RMB04946.1,
RC   ECO:0000313|Proteomes:UP000271227};
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 (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       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:RMB04946.1}.
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DR   EMBL; REFR01000012; RMB04946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0CDX9; -.
DR   InParanoid; A0A3M0CDX9; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000271227; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, 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:0000313|EMBL:RMB04946.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271227};
KW   Transferase {ECO:0000313|EMBL:RMB04946.1}.
SQ   SEQUENCE   441 AA;  47382 MW;  9317C1861CD69EF9 CRC64;
     MKSDTTPNSF VPGAVELPAE MQTAIARRGD AMGPAYRLSY ARPVAFVRGQ GVWLYDRDGN
     GYLDFYNNVV SLGHCHPRVV EAMHRQAALL CTNTRYLHDS VIQYSERLTR LFPAEMSQVM
     FCCSGSEAND LAFRIARHHT GGEGIIVTEH AYHGTTHVAS GMSPNLGVSV PLNPNVRTVQ
     APADCMNISG REQVGRIFAR DVQNAAADLR RQGIRPAALI VDTLFSSDGV FPDPSGFLAE
     AVDAIRAAGG LFIADEVQPG FARTGDAMWG FERHGVVPDI ATLGKPMGNG YPMAGLVVRP
     DVVESFGKGA RYFNTFAGNS VAAENGLAVL DVIRDEALLE NSATVGAYLK SVLTDIADDR
     IASVRGAGLF VGVEMRVPGG DAGESRDLAL GIVNALRDRR VLISTTGKYE TVLKIRPPLV
     TTSVHVDRFM EAFAAVLKET G
//