ID A0A0J5S4A2_9PAST Unreviewed; 377 AA.
AC A0A0J5S4A2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=TDP-4-oxo-6-deoxy-D-glucose aminotransferase {ECO:0000313|EMBL:KMK51617.1};
GN ORFNames=RO21_05405 {ECO:0000313|EMBL:KMK51617.1};
OS Muribacter muris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Muribacter.
OX NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK51617.1, ECO:0000313|Proteomes:UP000036270};
RN [1] {ECO:0000313|EMBL:KMK51617.1, ECO:0000313|Proteomes:UP000036270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK51617.1,
RC ECO:0000313|Proteomes:UP000036270};
RA Christensen H., Nicklas W., Bisgaard M.;
RT "Reclassification of Actinobacillus muris as Muribacter muris.";
RL Submitted (DEC-2014) 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:KMK51617.1}.
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DR EMBL; JWIZ01000027; KMK51617.1; -; Genomic_DNA.
DR RefSeq; WP_047976772.1; NZ_JWIZ01000027.1.
DR AlphaFoldDB; A0A0J5S4A2; -.
DR STRING; 67855.RO21_05405; -.
DR PATRIC; fig|67855.3.peg.947; -.
DR Proteomes; UP000036270; 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 InterPro; IPR012749; WecE-like.
DR NCBIfam; TIGR02379; ECA_wecE; 1.
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:KMK51617.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000036270};
KW Transferase {ECO:0000313|EMBL:KMK51617.1}.
FT ACT_SITE 182
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 182
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 377 AA; 42570 MW; C2BD7BB71C4F12F3 CRC64;
MHIPFNRPTL VGTELSYVQQ AMTSGQLAGN GEFSRRCERW FEQRFGTHKA LLAPSCTAAL
EMAAILLDIQ PDDEVIMPSY TFVSTANAFV LRGAKIVFVD VRPDTMNIDE RLIEQAITPK
TKAIVPVHYG GVACEMATIM ALAAKYRLWV VEDAAQAVMA RYRGKPLGTI GHLGCYSFHE
TKNYTAGGEG GAILINDPQL VARAEIVREK GTDRSRFFRG QVDKYRWQDV GSSFLLSDLQ
AAYLYAQLET ADLINQRRLT IWQRYFQAFS PLAETGELEL AAPPADCEHN AHLFYLKLAD
QTQREAFIQY LKRADILSVF HYVPLHTSPA GQRFGRFNGK DRYTTAESDR LVRLPLFFNL
TEQEAERVMK TAMAFFK
//
