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Database: UniProt
Entry: A0A0X3URU8_9ACTN
LinkDB: A0A0X3URU8_9ACTN
Original site: A0A0X3URU8_9ACTN 
ID   A0A0X3URU8_9ACTN        Unreviewed;       380 AA.
AC   A0A0X3URU8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Pyridoxal phosphate-dependent aminotransferase {ECO:0000313|EMBL:KUL35308.1};
GN   ORFNames=ADL15_14915 {ECO:0000313|EMBL:KUL35308.1};
OS   Actinoplanes awajinensis subsp. mycoplanecinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL35308.1, ECO:0000313|Proteomes:UP000053244};
RN   [1] {ECO:0000313|EMBL:KUL35308.1, ECO:0000313|Proteomes:UP000053244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL35308.1,
RC   ECO:0000313|Proteomes:UP000053244};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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 DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|ARBA:ARBA00037999, 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:KUL35308.1}.
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DR   EMBL; LLZH01000109; KUL35308.1; -; Genomic_DNA.
DR   RefSeq; WP_067690161.1; NZ_LLZH01000109.1.
DR   AlphaFoldDB; A0A0X3URU8; -.
DR   OrthoDB; 5342089at2; -.
DR   Proteomes; UP000053244; 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:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 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:KUL35308.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053244};
KW   Transferase {ECO:0000313|EMBL:KUL35308.1}.
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         191
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   380 AA;  40569 MW;  18B38C232E9B0EA3 CRC64;
     MTEPRIYLSP PHVTDVERKL LLEAFDSNWV APVGPDLNAF EAACAELVGV RHAVALSSGT
     AALHLALIAA GVRRGDTVLV PSFTFAASAN AVMYLGARPV FLDSTPESWN VDPQLVADEL
     RDRAGRGQLP RAVVTVDMYG QCADYQPILE ACDRYGVPLI EDAAEALGAT YRGRAAGSFG
     LAGVLSFNGN KIATTGGGGM LVTDDGSVAQ QVRHLATQAR EPVAHYEHRT VGYNYRLSNL
     LAAVGRGQMQ RLPAMIEARR ITAEHYRAAL GDLPGIAFIP VASYGVPNRW LTCLLVDAGK
     LGASRDQILA ALEKENIEAR PTWKPMHLQP AYRDCVVRGG AVAADLFHRG LCLPSGSALT
     GHDRDRVVTA VRSVAAGQRG
//
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