ID Q48I22_PSE14 Unreviewed; 408 AA.
AC Q48I22;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 96.
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 OrderedLocusNames=PSPPH_2771 {ECO:0000313|EMBL:AAZ36402.1};
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730 {ECO:0000313|EMBL:AAZ36402.1, ECO:0000313|Proteomes:UP000000551};
RN [1] {ECO:0000313|EMBL:AAZ36402.1, ECO:0000313|Proteomes:UP000000551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6 {ECO:0000313|Proteomes:UP000000551};
RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., Deboy R., Durkin A.S., Giglio M.G.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S., Crabtree J., Creasy T.,
RA Davidsen T., Haft D.H., Zafar N., Zhou L., Halpin R., Holley T., Khouri H.,
RA Feldblyum T., White O., Fraser C.M., Chatterjee A.K., Cartinhour S.,
RA Schneider D.J., Mansfield J., Collmer A., Buell C.R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
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; CP000058; AAZ36402.1; -; Genomic_DNA.
DR RefSeq; WP_004665403.1; NC_005773.3.
DR AlphaFoldDB; Q48I22; -.
DR KEGG; psp:PSPPH_2771; -.
DR eggNOG; COG0001; Bacteria.
DR HOGENOM; CLU_016922_1_5_6; -.
DR Proteomes; UP000000551; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}.
SQ SEQUENCE 408 AA; 43029 MW; 559EC5EB7E2ADB57 CRC64;
MKHLIGGISS GGRALPEIDG QAFNVARSNG PWLWDSKGVR YVDTAMGFGA TMLGHAQMEV
MAAASAAMLN GPMPSFAHAD EEAAAAALAT FTGDLSQVIF LNTGSEAVHL ACRTARVATG
RQRIVKFAAG YDGWYDSVAF GNAGQASALM SGTTRPERDG MLLLRYNDFE DAEQLFRDYS
DIAALVVEPV LANAGCIEPA PGYLKHLSDL AHRNGALVIL DEVLMGLRLC PGLTGTLLGA
EPDLATVGKA IGSGIPVAAL VGKPEYMRLF EQGKIVRAGT YSGAPPACAA VLATLKQLAT
ANYAALLTRG DQLRAQLVAA FASKGMAVSS TGYGSVFTLW PSATPPRTYA DAAHVADSEW
TLALHKALRR ERVMSMPFAF GRTYLTFAHQ EKALQAVLEG YKAAIASL
//
