ID Q7N0G9_PHOLL Unreviewed; 580 AA.
AC Q7N0G9;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
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=plu3919 {ECO:0000313|EMBL:CAE16291.1};
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01) (Photorhabdus luminescens subsp. laumondii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265 {ECO:0000313|EMBL:CAE16291.1, ECO:0000313|Proteomes:UP000002514};
RN [1] {ECO:0000313|Proteomes:UP000002514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01
RC {ECO:0000313|Proteomes:UP000002514};
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; BX571872; CAE16291.1; -; Genomic_DNA.
DR RefSeq; WP_011148054.1; NC_005126.1.
DR AlphaFoldDB; Q7N0G9; -.
DR STRING; 243265.plu3919; -.
DR GeneID; 24168865; -.
DR KEGG; plu:plu3919; -.
DR eggNOG; COG0001; Bacteria.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_016922_1_5_6; -.
DR OrthoDB; 9030879at2; -.
DR Proteomes; UP000002514; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR Gene3D; 1.10.1200.10; ACP-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; IPR036736; ACP-like_sf.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR009081; PP-bd_ACP.
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 Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000002514}.
FT DOMAIN 2..80
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 580 AA; 65638 MW; D6F7F4DBB2D3A113 CRC64;
MSNIEIIQRE IITIFAETFG LSKEEIKLEI PLVELGAESL LLFEALEPIH KQFGVKLSVR
QFFAELQTVR QLSEYILMVG KNRVVEDNHS VTQPVLSDQE KRSEQSDTSD IPPINKERFF
QWMLRSAPSI ESEERKKYLA SFISEYNERT IKSKIHSVAV RKNIADSRSG IGFKLSIKEL
LYPIVCTKFA GPVVKDIDGN DYIDMTMGFG AHLFGHSPPF VVKALTQQID NSFGLGTRHE
IGLEVAELIK EITGMDRVAF VNSGTEAVMN AVRAARALTR RNHIVLFSSS YHGHWDAVLA
RAGDYDEANA TKPVSVGIPE NMVADVSVFG FGSNEAIEFL KTNRTDIAAV LVEPVPTRDP
GLSNPDYLRH LRRVTRELDI LLIFDEIVTG FRSHPAGIQG LFGIEADIVI YGKTIGGGMP
LGVITGRKKM LDSIDGGNWN FNDDSFPAAE PTFFGGTYFQ HPLCMTAAKA TLQEIKRRGE
TFTKVLTQRT ESFVSRLNQL FLSRRVPIEA RSFSSFFRLM HRDNMDLLYY NLLMRGVYIW
EWRCWFISDA HDDTHLEKVY LAFVDSLDEL EENNLLPRYS
//
