ID A0A0W0WV70_9GAMM Unreviewed; 369 AA.
AC A0A0W0WV70;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Polysaccharide biosynthesis protein {ECO:0000313|EMBL:KTD36206.1};
GN ORFNames=Lnau_1190 {ECO:0000313|EMBL:KTD36206.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD36206.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD36206.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD36206.1,
RC ECO:0000313|Proteomes:UP000054725};
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|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:KTD36206.1}.
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DR EMBL; LNYO01000013; KTD36206.1; -; Genomic_DNA.
DR RefSeq; WP_058504224.1; NZ_LNYO01000013.1.
DR AlphaFoldDB; A0A0W0WV70; -.
DR STRING; 45070.Lnau_1190; -.
DR PATRIC; fig|45070.6.peg.1255; -.
DR OrthoDB; 9804264at2; -.
DR Proteomes; UP000054725; 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:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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}.
FT ACT_SITE 184
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 184
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 369 AA; 40836 MW; DEB49DA1F1DF5935 CRC64;
MQFIDLKKQY KLIEKDILRS IQTVLEHGQY IMGPEIGKLE LQLAEFLGVR HVIVNSSGTD
ALLMALLALD IEPGDEVITT PFSFFASAEV IALCQAKPVF VDIDPISYNI DVSKIEAAIT
PKTKAIMPVS LYGQCADMEI INRIAQKYGL PVIEDAAQSF GATYNGVYSG ALSTIGCTSF
FPSKPLGGYG DSGACFTDDD ILAEKLIEIR NHGQNVRYCH RRIGINGRMD TIQAAILIEK
LKLFPDEMIM RQKVAQRYQE LLSGLVRTPV VMPGNVSAYA QYTIEVPNRD EFQKNMQDLG
IPTATHYPVA IHQQQALKYL GYQVGDFPFA EKASKHVVSL PMHPYMSLEE QQTVANAVKK
SLVNELVGA
//
