ID A0A0W0Y5J7_9GAMM Unreviewed; 380 AA.
AC A0A0W0Y5J7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Polysaccharide biosynthesis protein {ECO:0000313|EMBL:KTD51951.1};
GN ORFNames=Lqui_0795 {ECO:0000313|EMBL:KTD51951.1};
OS Legionella quinlivanii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45073 {ECO:0000313|EMBL:KTD51951.1, ECO:0000313|Proteomes:UP000054618};
RN [1] {ECO:0000313|EMBL:KTD51951.1, ECO:0000313|Proteomes:UP000054618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC#1442-AUS-E {ECO:0000313|EMBL:KTD51951.1,
RC ECO:0000313|Proteomes:UP000054618};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD51951.1}.
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; LNYS01000006; KTD51951.1; -; Genomic_DNA.
DR RefSeq; WP_058506891.1; NZ_UGOX01000001.1.
DR AlphaFoldDB; A0A0W0Y5J7; -.
DR STRING; 45073.Lqui_0795; -.
DR PATRIC; fig|45073.5.peg.840; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000054618; 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 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 Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508};
KW Reference proteome {ECO:0000313|Proteomes:UP000054618}.
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 181
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 380 AA; 43155 MW; BFCB987564B581CF CRC64;
MILFNKPPYT TSEDHHVLAA MRSTKLCGDG HYTQLCQQWF EQQFHCKKAL LTPSCTAALE
MAAILLDIQP GDEVIMPSYT FVSTANAFVL RGATIVFVDI RPDTMNIDET KIEAAITDKT
KAIVPVHYAG VACEMNVIMA LAEKYQLYVV EDAAQAVMAF YEGRPLGTIG HFGCYSFHET
KNYTSGGEGG ALLINDERFI ERAEVIRQKG TNRTQFLKGQ VDKYTWRDLG SSFLPGELQA
AYLYSQLLEA KAINEQRLGI WNIYHDALAA YELNELITRP FIPEKCQHNA HMYYLKLPSF
ETRCDFIELM KRRGVQTAFH YVPLHSSPAG LKFGHFHGED DFTTNESEKL VRLPLWYNLE
PSEANFIIEQ VIDYFKPGNC
//