ID A0A1B9EVG6_9ACTN Unreviewed; 406 AA.
AC A0A1B9EVG6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose transaminase {ECO:0000313|EMBL:OCC11501.1};
DE EC=2.6.1.90 {ECO:0000313|EMBL:OCC11501.1};
GN Name=fdtB_1 {ECO:0000313|EMBL:OCC11501.1};
GN ORFNames=A3Q37_02698 {ECO:0000313|EMBL:OCC11501.1};
OS Streptomyces sp. PTY087I2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1819298 {ECO:0000313|EMBL:OCC11501.1, ECO:0000313|Proteomes:UP000093256};
RN [1] {ECO:0000313|EMBL:OCC11501.1, ECO:0000313|Proteomes:UP000093256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTY087I2 {ECO:0000313|EMBL:OCC11501.1,
RC ECO:0000313|Proteomes:UP000093256};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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|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:OCC11501.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LZRD01000010; OCC11501.1; -; Genomic_DNA.
DR RefSeq; WP_065482999.1; NZ_LZRD01000010.1.
DR AlphaFoldDB; A0A1B9EVG6; -.
DR PATRIC; fig|1819298.4.peg.2807; -.
DR Proteomes; UP000093256; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
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:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 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:OCC11501.1};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000093256};
KW Transferase {ECO:0000313|EMBL:OCC11501.1}.
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 210
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 406 AA; 43826 MW; 563DB70108576201 CRC64;
MPTNRSTVPR TTAALKIPFE PAQGGWYTGA EHDAIRMAMS SSEDWRTGWR GGEYVTSFED
AFARYTGASH ALAFNSGGTA MEMVLRALEL KPGDEVISCA INFVGPHIAV IGQGGRLVLA
EPDPVTLNLD LADTEQRIGP QTRAILVTHW NGASADIGRF VELAARHPHP VHGPPVVIVD
AARACGGRTP SGARVGSEGW ATVFSFESKK LMTTFGQGGM VTTDDHVLAE RLRGLRTYGG
RAGWGTNQLL TKAQAAVGLI QLARLDEMNA ARITRAHDRT AALADIPELT LPPTLDEGLH
LYYRHNLLVP EAWAGRGRDE LMDVLADRYG VGSIVSDPVT YLGHDLIRAH TAGQHCPRAK
QLAARLLCPC LHPQMTEDEE AQVRNAIRRA VAGTAQLHPV IVKENG
//
