ID A0A2T6C985_9BACL Unreviewed; 411 AA.
AC A0A2T6C985;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=dTDP-4-amino-4,6-dideoxygalactose transaminase {ECO:0000313|EMBL:PTX64898.1};
GN ORFNames=C8P63_101118 {ECO:0000313|EMBL:PTX64898.1};
OS Melghirimyces profundicolus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Melghirimyces.
OX NCBI_TaxID=1242148 {ECO:0000313|EMBL:PTX64898.1, ECO:0000313|Proteomes:UP000244240};
RN [1] {ECO:0000313|EMBL:PTX64898.1, ECO:0000313|Proteomes:UP000244240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45787 {ECO:0000313|EMBL:PTX64898.1,
RC ECO:0000313|Proteomes:UP000244240};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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:PTX64898.1}.
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DR EMBL; QBKR01000001; PTX64898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6C985; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000244240; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
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: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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000244240}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 198
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 411 AA; 45776 MW; B46CA805E43121F1 CRC64;
MGNEQLAIHG GPKVKTKPFG TGKRFGDEEI RELKEALDQN TLFYHSGNKV KTFLERFNEL
YGIRYSVAAS SGTAAIHVAL GAAGVSVGDE VITSPITDQG TLIGILYQNA IPVFADLDPR
TYNMDPKSIV DRITPKTKAI LVVHLAGNPA DMDAVMDIAR RYKLKVVEDC AQSYMTRYKG
RCVGTIGDYG CFSTNDFKHI STGDGGLVTV NSGKEEDFRV VHAFADKNYQ RLQGEVFREL
NYLAPNYRMT ELQGAVGIAQ LKKLPEICEK RHQYGERMTE GIRDLPGILP PKVTEGGWSS
YWFYMLRLDG SRLNCTREVF SSALGAEGIP NHPGYIPEVV YRQPLFQKRQ AYPGSDFPFC
LSETSYQPGI CPEAEQILAT AVRLPISEFF TESDIEDMVR GIRKVALHYA K
//
