ID E1SEI1_PANVC Unreviewed; 412 AA.
AC E1SEI1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Aminotransferase class-V {ECO:0000313|EMBL:ADO08472.1};
DE EC=2.6.1.- {ECO:0000313|EMBL:ADO08472.1};
GN Name=pucG {ECO:0000313|EMBL:ADO08472.1};
GN OrderedLocusNames=Pvag_0258 {ECO:0000313|EMBL:ADO08472.1};
OS Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO08472.1, ECO:0000313|Proteomes:UP000006631};
RN [1] {ECO:0000313|EMBL:ADO08472.1, ECO:0000313|Proteomes:UP000006631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C9-1 {ECO:0000313|EMBL:ADO08472.1,
RC ECO:0000313|Proteomes:UP000006631};
RX PubMed=20952567; DOI=10.1128/JB.01122-10;
RA Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA Stockwell V.O., Frey J.E., Duffy B.;
RT "The genome sequence of the biocontrol agent Pantoea vagans strain C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR000524-50};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00009236}.
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DR EMBL; CP002206; ADO08472.1; -; Genomic_DNA.
DR AlphaFoldDB; E1SEI1; -.
DR KEGG; pva:Pvag_0258; -.
DR eggNOG; COG0075; Bacteria.
DR HOGENOM; CLU_027686_0_0_6; -.
DR Proteomes; UP000006631; Chromosome.
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; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase.
DR PANTHER; PTHR21152:SF39; ALANINE--GLYOXYLATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR21152; AMINOTRANSFERASE CLASS V; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF000524; SPT; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:ADO08472.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000524-50};
KW Transferase {ECO:0000313|EMBL:ADO08472.1}.
FT DOMAIN 45..352
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-1"
FT MOD_RES 201
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000524-50"
SQ SEQUENCE 412 AA; 45387 MW; E87C7A3546D82A9C CRC64;
MMDITKFPQL NPPQRLLMGP GPINADPRVL RAMSSQLLGQ YDPAMTHYMN EVMALYRGVF
RTENRWTLLI DGTSRAGIEA ILLSSIRPGD KVLVPVFGRF GHLLCEIARR CRADVHTIEV
PWGEVFTPDQ IEDAIKKVRP RLLLTVQGDT STTMLQPLEQ LGAICKQYGV LFYTDATASL
AGNALETDAW GLDAVSAGMQ KCLGGPSGTS PVTLSAEMEA VIRKRKCVEQ GIRTEAHQDG
EEEMIYSNYF DLGMIMDYWG PERLNHHTEA TSALFGAREC ARLILQEGLD NGIARHKLHG
EAMLKGIQGM GLETFGDLKN KMNNVLGVMI PSGVNGDQVR KLMLEDFGIE IGTSFGPLHG
KVWRIGTMGY NARKDCVMQT LSALETVLTY VGYRTPQGAA AQAAWDHYGS HA
//
