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Database: UniProt
Entry: A0A0W0XVU6_9GAMM
LinkDB: A0A0W0XVU6_9GAMM
Original site: A0A0W0XVU6_9GAMM 
ID   A0A0W0XVU6_9GAMM        Unreviewed;       743 AA.
AC   A0A0W0XVU6;
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=Aminotransferase class-III {ECO:0000313|EMBL:KTD48714.1};
DE            EC=2.6.1.44 {ECO:0000313|EMBL:KTD48714.1};
GN   ORFNames=Lrub_1065 {ECO:0000313|EMBL:KTD48714.1};
OS   Legionella rubrilucens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=458 {ECO:0000313|EMBL:KTD48714.1, ECO:0000313|Proteomes:UP000054608};
RN   [1] {ECO:0000313|EMBL:KTD48714.1, ECO:0000313|Proteomes:UP000054608}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WA-270A-C2 {ECO:0000313|EMBL:KTD48714.1,
RC   ECO:0000313|Proteomes:UP000054608};
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954}.
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:KTD48714.1}.
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DR   EMBL; LNYT01000007; KTD48714.1; -; Genomic_DNA.
DR   RefSeq; WP_058531157.1; NZ_LNYT01000007.1.
DR   AlphaFoldDB; A0A0W0XVU6; -.
DR   STRING; 458.Lrub_1065; -.
DR   PATRIC; fig|458.5.peg.1102; -.
DR   Proteomes; UP000054608; Unassembled WGS sequence.
DR   GO; GO:0008453; F:alanine-glyoxylate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1200.10; -; 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; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KTD48714.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054608};
KW   Transferase {ECO:0000313|EMBL:KTD48714.1}.
FT   DOMAIN          26..248
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   743 AA;  82095 MW;  C56526D719A21FE1 CRC64;
     MFTSPDAQQL LLDHYRLNAV AIPLPGESDC NFHIKTTAGD EYLLKVSKAE DQEAIIQLQN
     SALAWLQRFP RPFGFPQLLP LATGEATGRV LSSQGEPCHV RLFTFVQGQL LVNVPCSTAL
     VHQLGRAAGH LTQALAGFRH AAAARQLKWD LRQAEWIENE VQAIEHPDDR RLVSDFLAEF
     KRDTAPLLPD LRQSIIHGDL NDYNIVVQAH QIGFIDFGDL LQTATICELA IALAYTLMHR
     SDALAAAMEM IRSYHRVFPL EEREVDVLYS LVAMRLCVSV VNSALRKKEN PGNAYLTVSE
     QPAWHLLKQW RSIDPQWALL CFRQACGFMD KHLSNKESLL SLRKKVIADN VGLSYQQPLE
     IVRGEGAYLY DETGRPYLDC VNNVCHVGHC HPRVVQAGQQ QMALLNTNTR YLHRYLLDYA
     QRLLATLPLP LDVCFFVSSG SEANELALRL AYTHTRSRKT WVIDHAYHGN TTTLINISPY
     KFKQKGGQGK PDWVTVLPMP DPLRGPVNPL FSLPTEPTVF IAESLLSCGG QIELPPGYLD
     AIYTAIRSTG GVCIADEVQV GLGRVGSHVW GFETQGVVPD IVTMGKPLGN GHPIGAVVTT
     RAIAASFSQG MEYFSTFGGN PVSCAIGLSV LDVLEEECLQ AKAWSTGHYL KQRLLGLKNR
     YDCIADVRGL GLFLGVELTK KGGVEPDGDF TGKLVNRMKD LGVLLSRDGP HHNVLKIKPP
     LVFGSAHADN LVDTLDKALA SLL
//
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