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
//
