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Database: UniProt
Entry: A0A0M8VSJ3_9ACTN
LinkDB: A0A0M8VSJ3_9ACTN
Original site: A0A0M8VSJ3_9ACTN 
ID   A0A0M8VSJ3_9ACTN        Unreviewed;       394 AA.
AC   A0A0M8VSJ3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=dTDP-4-dehydro-6-deoxyglucose aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ADL00_07610 {ECO:0000313|EMBL:KOV71430.1};
OS   Streptomyces sp. AS58.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV71430.1, ECO:0000313|Proteomes:UP000037758};
RN   [1] {ECO:0000313|EMBL:KOV71430.1, ECO:0000313|Proteomes:UP000037758}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS58 {ECO:0000313|EMBL:KOV71430.1,
RC   ECO:0000313|Proteomes:UP000037758};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KOV71430.1}.
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DR   EMBL; LGDU01000047; KOV71430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8VSJ3; -.
DR   PATRIC; fig|1519489.3.peg.1783; -.
DR   Proteomes; UP000037758; Unassembled WGS sequence.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; 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:SF9; PROTEIN RV3402C; 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   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR000390-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037758}.
FT   ACT_SITE        205
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         205
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   394 AA;  42261 MW;  A53F175D1AC72485 CRC64;
     MAGGVVRTKR TRSDLAYYGG TPGFAEDIRV GTPNVPAKDR YLELVGEAID RRWLSNLGPL
     VRRFEALAAE RTLRAHNTAT NNATTALQVA VKACGVTGEV IMPSFTFVAS AHAMDWIGLT
     PVFADVDPET GTLDPRSVAK AVSPRTGGIL GVHIWGNLCD TAGLDDVARE AGVPLVFDSA
     QAFGCLPLRP APAGAAEVFS FHATKILNCF EGGLVATDSA EVHARVRSMH NFGFDETMDV
     VGPGTNAKMN ESSAAMGIAS VEHLDDMLKV YRALYARYRT GLADVPGVSL MAAPEGQTHN
     HQYVVVRVDP EAAGLDRDRL MAVLDAENVR TKKYFSPGCH TMPPYRRETV HTPVDLSVTE
     TLTERVLALP TGLSVTPDDV DRICDVIAAA VRYA
//
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