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Database: UniProt
Entry: A0A2S4MIC2_9BURK
LinkDB: A0A2S4MIC2_9BURK
Original site: A0A2S4MIC2_9BURK 
ID   A0A2S4MIC2_9BURK        Unreviewed;       428 AA.
AC   A0A2S4MIC2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:POR54498.1};
GN   ORFNames=B0G62_102106 {ECO:0000313|EMBL:POR54498.1};
OS   Paraburkholderia eburnea.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1189126 {ECO:0000313|EMBL:POR54498.1, ECO:0000313|Proteomes:UP000237381};
RN   [1] {ECO:0000313|EMBL:POR54498.1, ECO:0000313|Proteomes:UP000237381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 18070 {ECO:0000313|EMBL:POR54498.1,
RC   ECO:0000313|Proteomes:UP000237381};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JAN-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   -!- 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:POR54498.1}.
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DR   EMBL; PQGA01000002; POR54498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4MIC2; -.
DR   Proteomes; UP000237381; Unassembled WGS sequence.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
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; IPR004632; 4NH2But_aminotransferase_bac.
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   NCBIfam; TIGR00700; GABAtrnsam; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:POR54498.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237381};
KW   Transferase {ECO:0000313|EMBL:POR54498.1}.
SQ   SEQUENCE   428 AA;  45728 MW;  B5FBA46C07844222 CRC64;
     MSKNADLQSR KDAITPRGVG VMCNFYAERA ENAELWDVEG RRFIDFAAGI AVCNTGHRHP
     KIVAAIKAQL DQFTHTAYQI VPYESYVSLA EKVAQRAPGS FAKKAAFFTT GAEAVENAVK
     IARASTGRPG VIAFAGGFHG RTMMGMALTG KVAPYKLNFG PFPADVYHAP YPNSVHGIST
     ADSLKHIEML FKADIDPKRV AAIIFEPVQG EGGFYQAPAD FVRGLRKICD THGILLIADE
     VQTGFARTGK LFAMEHYDVA PDLMTIAKSL AGGMPLSGVV GRAEVMDAAA PGGLGGTYAG
     NPLAVASAHA VIEIIEEEKL CERATKLGDK IKAKLNAMKA EVPQIADVRG PGAMNAVEFC
     KPGTNEADAD FTKRVQTAAL NRGLLLLVCG VYSNVVRFLF PLTIQENVFD EALAILEESI
     KEAVGVPA
//
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