ID W7LHD2_GIBM7 Unreviewed; 436 AA.
AC W7LHD2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0000313|EMBL:EWG37906.1};
GN ORFNames=FVEG_01314 {ECO:0000313|EMBL:EWG37906.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG37906.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG37906.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(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; DS022242; EWG37906.1; -; Genomic_DNA.
DR RefSeq; XP_018744097.1; XM_018888229.1.
DR AlphaFoldDB; W7LHD2; -.
DR STRING; 334819.W7LHD2; -.
DR GeneID; 30059621; -.
DR KEGG; fvr:FVEG_01314; -.
DR VEuPathDB; FungiDB:FVEG_01314; -.
DR eggNOG; KOG1401; Eukaryota.
DR OrthoDB; 1445768at2759; -.
DR Proteomes; UP000009096; Chromosome 1.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009096}.
SQ SEQUENCE 436 AA; 47294 MW; 70984104DCE3606C CRC64;
MSSELIQQIQ AELEAATTRY IDRNPRSRAL HDEALKSMPG GNTRTVLHAS PFPVVIKSGQ
GHQITSEDGH AYTDFTGEFT AALYGHSNPV IISAIRDVLD NVGMNVGGNT AQEQIFAREI
CSRFNLQHVR FCNSGTEANI HALAAARAFT NKRKVVTFSG GYHGAVIGFK GVNPEANNVD
LDDWVVARYN DLDSARAAIE SEGVAAVLVE GMQGSGGGIP GHPEFLQGIQ EIARNAGALF
IIDEVMTSRL SGGGISEMRG LKPDLKTFGK YLGGGLAFGA FGGRADIMAA FDPRLPTALS
HSGTFNNNTL VTHTGYAGLT KVYTPEVAAQ FTRSGDELRD RLNAVTKGTR VLFTGIGTIM
GIHFPKDGSR VIERSGEVEE LDSLRDLFWL DMMEEGFWIV RRGFMALVLD TPMGEFDRFV
SCVEAWVSKR AEMVKI
//
