ID A0A0W0WKK0_9GAMM Unreviewed; 436 AA.
AC A0A0W0WKK0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:KTD32861.1};
DE EC=2.6.1.44 {ECO:0000313|EMBL:KTD32861.1};
GN ORFNames=Lnau_2509 {ECO:0000313|EMBL:KTD32861.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD32861.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD32861.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD32861.1,
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 -!- 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 ECO:0000256|RuleBase:RU003560}.
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:KTD32861.1}.
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DR EMBL; LNYO01000024; KTD32861.1; -; Genomic_DNA.
DR RefSeq; WP_058505503.1; NZ_LNYO01000024.1.
DR AlphaFoldDB; A0A0W0WKK0; -.
DR STRING; 45070.Lnau_2509; -.
DR PATRIC; fig|45070.6.peg.2646; -.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000054725; 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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
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 PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:KTD32861.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KTD32861.1}.
SQ SEQUENCE 436 AA; 47305 MW; DC9AE448FFD88122 CRC64;
MHENNDSALI NFRKNHFLPT AALYYKKPVQ LTKAQGVYAW DAEGKRYLDA IGGIVCISAG
HNHPKIKKAL INAIENDSIQ HTSLLYLHQA PVETAKHLLE DAPKGMDRVS FTNSGSEANE
LAIMAARHAT GETMVVNVRH SYHGGTSATL ASCGLSIWRF KAQPVTAVTS ALEPYCYRCP
FKQKPESCAL ECAKNVETTI QNSTHGKIAA FILEPIMGVG GFITPPEAYF SEVARIVHNY
GGKYISDEVQ TGAGRCGGDF LLTKTLGIDA DIVTMAKGFG NGAAVGAVLM KTEVAESMAG
KTYFNTFAGD PLQMIQAKLT MEIIKEEQLV ENARTMGELL KDGLNQLAKK HALIGDVRGR
GLLLGVELVK DRNTKTPATE ETAQLMELCK DKGLLIGKGG QWGSVLRIAP PLTINREEVN
FMLETLDRAL VELSSA
//
