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
//