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Database: UniProt
Entry: A0A0W0Y5J7_9GAMM
LinkDB: A0A0W0Y5J7_9GAMM
Original site: A0A0W0Y5J7_9GAMM 
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}.
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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
//
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