ID   A0A402DU67_9CELL        Unreviewed;       379 AA.
AC   A0A402DU67;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Pyridoxal phosphate-dependent aminotransferase {ECO:0000313|EMBL:GCE77699.1};
GN   ORFNames=CBZ_27550 {ECO:0000313|EMBL:GCE77699.1};
OS   Cellulomonas biazotea.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1709 {ECO:0000313|EMBL:GCE77699.1, ECO:0000313|Proteomes:UP000289954};
RN   [1] {ECO:0000313|EMBL:GCE77699.1, ECO:0000313|Proteomes:UP000289954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC12680 {ECO:0000313|EMBL:GCE77699.1,
RC   ECO:0000313|Proteomes:UP000289954};
RA   Yamamura H., Hayashi T., Hamada M., Serisawa Y., Matsuyama K., Nakagawa Y.,
RA   Otoguro M., Yanagida F., Hayakawa M.;
RT   "Draft genome sequence of Cellulomonas takizawaensis strain TKZ-21.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
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:GCE77699.1}.
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DR   EMBL; BIMR01000239; GCE77699.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A402DU67; -.
DR   OrthoDB; 9804264at2; -.
DR   Proteomes; UP000289954; Unassembled WGS sequence.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:GCE77699.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:GCE77699.1}.
FT   ACT_SITE        184
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         184
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   379 AA;  40236 MW;  24C84923C075AEAC CRC64;
     MTEVVPLGQP TVGAEELEAI AEVFASGWLS GAGPACQAFE AEFAAVSGTE HVLATSNCGS
     ALHLGLDVLG AGPGDEVIVG DYTFPATGHS VMWTGATPVF ADVRPDIWSA DPASVEASIT
     ERTVGIVAVD VFGQPADYDE LRAIADKHGL WLMEDAACSA GATYKGRPAG SLADVATFSF
     HGRKGITAGE GGALTTDRED LARHARKLHT YGIEPALSRE GARELPVPSF DEAGYNYRLS
     DVAAAIMRVQ VRRLPELLAN RRRAAAGYAE LLGDLDLVTL PAALDDREHP WQSYVLTLDP
     SLDRGVVALE LRARGVQCNF GTYASHVQPV YGGRQSLPVS ADLFARHLAV PMHANLTDAQ
     VERVAEVVRD VVTAPTSRR
//