ID   E7BB56_LEGPN            Unreviewed;       429 AA.
AC   E7BB56;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000256|ARBA:ARBA00015416};
DE   AltName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000256|ARBA:ARBA00031365};
GN   ORFNames=LPSG12_007 {ECO:0000313|EMBL:CBY79952.1};
OS   Legionella pneumophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=446 {ECO:0000313|EMBL:CBY79952.1};
RN   [1] {ECO:0000313|EMBL:CBY79952.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43290 {ECO:0000313|EMBL:CBY79952.1};
RA   Merault N., Rusniok C., Jarraud S., Gomez-Valero L., Cazalet C., Marin M.,
RA   Brachet E., Aegerter P., Gaillard J.L., Etienne J., Herrmann J.L.,
RA   Lawrence C., Buchrieser C.;
RT   "A specific real-time PCR for simultaneous detection and identification of
RT   Legionella pneumophila serogroup 1 in water and clinical samples.";
RL   Appl. Environ. Microbiol. 77:1708-1717(2010).
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|RuleBase:RU003560}.
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DR   EMBL; FR747826; CBY79952.1; -; Genomic_DNA.
DR   RefSeq; WP_014326751.1; NZ_RBEZ01000012.1.
DR   AlphaFoldDB; E7BB56; -.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43713; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE; 1.
DR   PANTHER; PTHR43713:SF3; GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE 1, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:CBY79952.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CBY79952.1}.
SQ   SEQUENCE   429 AA;  48128 MW;  C2A3F3A9E95D9A07 CRC64;
     MYKCYEASER FLERALESIP LGSQTFSKSY VQFPKGVSPL FLQRGAGCKV WDLDGNEYTD
     FVNGLLAVTL GYNDPDVNAS VLEQLQNGVT FSLAHPLETM VAEKLIETIP CAEMVRFGKN
     GSDVTSGAIR LARAYTNKDR IAVCGYHGWQ DWYIGTTPRN LGVPKSTQEL THTFAYNDTD
     SLDRLFSAYP GQFAAVIMEP MNIEQPKSGF LESVKELAHH HGALLIFDEM ITGFRFAIGG
     AQSYFNVLPD LATFGKGMAN GYPLAALVGR KDIMQLMTEI FFSFTFGGET LSLAASYATI
     NKIQSQPVIE KLFTLGTQLK EGIHQLIDKY SMDSFLSCVG HPSWSFLIFK DIEPYTSWDI
     KTLWMQEILA RGILSFGTHN LSYAHNECDI DNLLKIYNQV FPLLREAVVQ KNLHKLLRAE
     PLQPLFKVR
//