ID   B4RDM1_PHEZH            Unreviewed;       428 AA.
AC   B4RDM1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ACG78411.1};
GN   OrderedLocusNames=PHZ_c2000 {ECO:0000313|EMBL:ACG78411.1};
OS   Phenylobacterium zucineum (strain HLK1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG78411.1, ECO:0000313|Proteomes:UP000001868};
RN   [1] {ECO:0000313|EMBL:ACG78411.1, ECO:0000313|Proteomes:UP000001868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLK1 {ECO:0000313|EMBL:ACG78411.1,
RC   ECO:0000313|Proteomes:UP000001868};
RX   PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA   Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT   "Complete genome of Phenylobacterium zucineum - a novel facultative
RT   intracellular bacterium isolated from human erythroleukemia cell line
RT   K562.";
RL   BMC Genomics 9:386-386(2008).
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}.
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DR   EMBL; CP000747; ACG78411.1; -; Genomic_DNA.
DR   RefSeq; WP_012522553.1; NC_011144.1.
DR   AlphaFoldDB; B4RDM1; -.
DR   STRING; 450851.PHZ_c2000; -.
DR   KEGG; pzu:PHZ_c2000; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_5; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000001868; Chromosome.
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   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:ACG78411.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001868};
KW   Transferase {ECO:0000313|EMBL:ACG78411.1}.
SQ   SEQUENCE   428 AA;  44821 MW;  57A1F3A132DEACCA CRC64;
     MSRNAELLSR RTAAVSRGVS TATPVFAARA ENAEIWDADG RRYVDFAGGI AVLNVGHRHP
     KVIEAVRAQL DAYTHTAFQV MAYEPYIELA ERLNALAPFK GPAKTLFFTT GAEAVENAVK
     IARVATGRTA VIAFTGAFHG RTMLTMGLTG KVAPYKKNFG PSPAELYHLP FPGSRAGVSV
     DDTLRALDLL FAADVAPDRV AAIIIEPVQG EGGFNPAPVE LMTALRRVCD EHGILLIADE
     VQTGFARTGK MFGIEHYPVE PDLVPVAKSL AGGFPLSGVI GRADLMDVVD PGGLGGTYGG
     SPVACAAALA VLDVIAEEGL LERAGAIGSA MRRRLSAIAA RNDVAPISEP RGPGAMVAFD
     MLKSRGGDEP DGAAAKAVVS RALDAGLVLL SCGRYGETIR LLVPLTVSDE VLAEGMDILE
     GALRDVAP
//