ID   A0A094ACZ3_9PEZI        Unreviewed;       459 AA.
AC   A0A094ACZ3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=V493_03443 {ECO:0000313|EMBL:KFY27511.1};
OS   Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY27511.1, ECO:0000313|Proteomes:UP000029327};
RN   [1] {ECO:0000313|EMBL:KFY27511.1, ECO:0000313|Proteomes:UP000029327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KFY27511.1}.
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DR   EMBL; JPJV01001342; KFY27511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094ACZ3; -.
DR   STRING; 1420906.A0A094ACZ3; -.
DR   HOGENOM; CLU_016922_1_2_1; -.
DR   OrthoDB; 1445768at2759; -.
DR   Proteomes; UP000029327; Unassembled WGS sequence.
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:UP000029327}.
SQ   SEQUENCE   459 AA;  49083 MW;  4E27447530A42B1C CRC64;
     MASADSNVQD ALRDATAEFV TANTASESVF NRASGHLPAG NTRTTLFSPP FPLAITIASG
     CSIRSADGDV YLDMVGEYTA GIYGHSHPDI LEALEGALVN GVNFGATSAL EGELAARIKK
     RFQAGAGLEM VRFTNSGTEA NILATTTARA WTGRSKILVF AGSYHGSVLS FHTKGKLDPM
     TMPGEYVVAD YNSIESFEEE LSQISADSLA AILVEPMQGA GGCLPASVEF LQHLRARATE
     LKALLIFDEV MTSRLHHAGG LAGKYGIKPD LMTMGKYLGG GMSFGLFGGR REIMELFNPK
     SGGVVTMADG TQTPMSLAHS GTFNNNVLTM HAGIAGTKIL TEPVLTQLNE LGDHLRRAVL
     SILVAKGLVS AAIEADMRDI ATVPRGRIWI SGVGSINAIH FGADDELVDL RDLFYFHMIK
     NNIYVTRRGF VALSIVHTKD DIDRYVKCVA SFVDRWAGA
//