ID J0TZZ9_9BURK Unreviewed; 437 AA.
AC J0TZZ9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Glutamate-1-semialdehyde aminotransferase {ECO:0000313|EMBL:EJE49477.1};
GN ORFNames=PMI14_05956 {ECO:0000313|EMBL:EJE49477.1};
OS Acidovorax sp. CF316.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE49477.1, ECO:0000313|Proteomes:UP000004811};
RN [1] {ECO:0000313|EMBL:EJE49477.1, ECO:0000313|Proteomes:UP000004811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF316 {ECO:0000313|EMBL:EJE49477.1,
RC ECO:0000313|Proteomes:UP000004811};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
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:EJE49477.1}.
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DR EMBL; AKJX01000229; EJE49477.1; -; Genomic_DNA.
DR RefSeq; WP_007859732.1; NZ_AKJX01000229.1.
DR AlphaFoldDB; J0TZZ9; -.
DR PATRIC; fig|1144317.3.peg.5491; -.
DR Proteomes; UP000004811; Unassembled WGS sequence.
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:EJE49477.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000004811};
KW Transferase {ECO:0000313|EMBL:EJE49477.1}.
SQ SEQUENCE 437 AA; 46105 MW; 80FE56ECE48F1E28 CRC64;
MNATPAPLDH ALFQAVENYR ARNPRSAALL AEAETALPGG NTRSVLFHGP FPLSMARGAG
CRVWDADGHE YIDALGEFTA GLYGHSHPVV LAAIEEALRG GINLSSHTAR EGLLAHEIQR
RFPSMELLRF ANSGTEANLL ALAAAKAHTG RSKVVVFDGA YHGGVLTFSG GGSPMNVPHD
FVLARYNDAD SVRALVAAHG PDIAAILVEP MLGAGGCIPG EPAFLQALRT LADECGALLV
FDEVMTSRLS FGGRQALLSI RPDLTTAGKY LGGGMSFGVF GGRRDVMERF DPRRPDALAH
AGTFNNNVLT MAAGHAGLIQ VLTAEVVQAL NERGEQLRAR FNAVLERHGV DMAFTGTGSL
MTLHATAAPV RSPADLQGTD GRAKDLVFFG LLEEGVFMAR RGLIALSLPV GDAECDALVA
ALEAVVVRHR AVLPARA
//
