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Database: UniProt
Entry: A0A238ZS86_9ACTN
LinkDB: A0A238ZS86_9ACTN
Original site: A0A238ZS86_9ACTN 
ID   A0A238ZS86_9ACTN        Unreviewed;       357 AA.
AC   A0A238ZS86;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=dTDP-4-amino-4,6-dideoxygalactose transaminase {ECO:0000313|EMBL:SNR85533.1};
GN   ORFNames=SAMN06264365_106222 {ECO:0000313|EMBL:SNR85533.1};
OS   Actinoplanes regularis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=52697 {ECO:0000313|EMBL:SNR85533.1, ECO:0000313|Proteomes:UP000198415};
RN   [1] {ECO:0000313|EMBL:SNR85533.1, ECO:0000313|Proteomes:UP000198415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43151 {ECO:0000313|EMBL:SNR85533.1,
RC   ECO:0000313|Proteomes:UP000198415};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; FZNR01000006; SNR85533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238ZS86; -.
DR   Proteomes; UP000198415; Unassembled WGS sequence.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198415}.
FT   ACT_SITE        170
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         170
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   357 AA;  37643 MW;  46BEDAFE514908DC CRC64;
     MAALRSGWVA PAGPDLDRFE REIADRVGVP HAVAVNSGTS ALHLALIGAG AGPGDVVVVP
     TLTFAATANA VVYTGATPVF ADCDPVTGNL DPDVLSGLLA ELSAEGAPVR AVLTVDLYGF
     CADYDRILPL CDRYGVPLIE DATEALGAAY RGRAAGSFGW AAALSFNGNK IMTTSSGGML
     LTADPGLATR ARNLASQARL PVAHYEHAEI GYNYRLSNLL AALGRAQLCR LDEMIERRRT
     IRDGYAKVFA NLDGVRLLSG DDPGANCWLT GVVVDPERAG WSARDLAAHL AARNVETRPV
     FKPMHLQPVF AGSRAALTGA AEHLFDDGLV LPSGSVLADG QVRRVLDEIT EFLDGRR
//
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