ID K9DNT5_9BURK Unreviewed; 405 AA.
AC K9DNT5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=UDP-4-keto-6-deoxy-N-acetylglucosamine 4-aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9710_04238 {ECO:0000313|EMBL:EKU80452.1};
OS Massilia timonae CCUG 45783.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU80452.1, ECO:0000313|Proteomes:UP000009874};
RN [1] {ECO:0000313|EMBL:EKU80452.1, ECO:0000313|Proteomes:UP000009874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU80452.1,
RC ECO:0000313|Proteomes:UP000009874};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Massilia timonae CCUG 45783.";
RL Submitted (SEP-2012) 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:EKU80452.1}.
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DR EMBL; AGZI01000051; EKU80452.1; -; Genomic_DNA.
DR RefSeq; WP_005669812.1; NZ_JH992925.1.
DR AlphaFoldDB; K9DNT5; -.
DR PATRIC; fig|883126.3.peg.4273; -.
DR eggNOG; COG0399; Bacteria.
DR HOGENOM; CLU_033332_0_3_4; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000009874; Unassembled WGS sequence.
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:UP000009874}.
FT ACT_SITE 195
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 405 AA; 43800 MW; 807F90074DB92651 CRC64;
MPDHTASASA ADTFLPFALP DIGEEEIRAV EACLRSGWVT TGPVTRRFET AFRDYLGGEV
EAIAVNSATA GLHLALEAAG VGPDDEVIVP TLTFTASAEV VRYLGARPVF VDADPHTLNL
DPAAVAAAIT PRTRAIVAVH FAGMAADMDA IGRLARRHGL RVIEDAAHAF PTRHRGRLVG
TLDSDVTVFS FYANKTMTTG EGGMVVTRDP RLAERIRCMR LHGISRDAFD RYTARTPSWY
YEVVAAGFKY NLTDIASAIG IEQLRKIDRF QQRRTALAER YDAALAGLPL TLPARPAPGS
GSTHAWHLYV VRLDRAAADG ADSASTAQRE RDALIANLAE RGIGTSVHFI PLHRQPYWRG
SCGLRAADFP VAEAAFGAML SLPLYTRMGD ADQQRVIAAL HDLLS
//