ID A0A0Q5E7C4_9MICO Unreviewed; 402 AA.
AC A0A0Q5E7C4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=TDP-4-oxo-6-deoxy-D-glucose aminotransferase {ECO:0000313|EMBL:KQQ52475.1};
GN ORFNames=ASF68_09135 {ECO:0000313|EMBL:KQQ52475.1};
OS Plantibacter sp. Leaf314.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Plantibacter.
OX NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ52475.1, ECO:0000313|Proteomes:UP000051200};
RN [1] {ECO:0000313|EMBL:KQQ52475.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52475.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ52475.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52475.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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|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:KQQ52475.1}.
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; LMOB01000001; KQQ52475.1; -; Genomic_DNA.
DR RefSeq; WP_056009484.1; NZ_LMOB01000001.1.
DR AlphaFoldDB; A0A0Q5E7C4; -.
DR STRING; 1736333.ASF68_09135; -.
DR Proteomes; UP000051200; 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: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:KQQ52475.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000051200};
KW Transferase {ECO:0000313|EMBL:KQQ52475.1}.
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 190
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 402 AA; 43131 MW; E847E0F9AD9CD8EF CRC64;
MMAEVGISPR IPLSKPYRAA GELEQLEQVL ASDHVHGDGR FTASASDRLR HLTGAQHVLL
TTSGTHALEM MTRLIGVGPG DEVILPSFTF PSAANAVVLA GATPVFVDSD PTTGNLDPQH
VADAIGPRTR AISVMHYGGV PVDVPAFLGL AAEHGLHLLE DNAHGLGVSG AGVRLGTVGT
MAAQSFHDTK NVHCGEGGAL LINDESVLLR AEIMREKGTD RAQFLRGQVD KYSWADLGSS
YLPSELNAAV LDTQLRDFDV IQAHRHRIWD RYAAELAEWA HDRGATLMDP PGGVHAAHLF
FLLLPDAEVQ QEFLRHLQAH GIGAAFHYVP LHSSAAGRRY GRVVSEPQHA VRFAERLVRL
PLWPAMTDAE VDRVVAAVRA FGATPDLTAA TTASTGQDSI WA
//
