ID B6QKY6_TALMQ Unreviewed; 438 AA.
AC B6QKY6;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Glutamate-1-semialdehyde 2,1-aminomutase, putative {ECO:0000313|EMBL:EEA21763.1};
GN ORFNames=PMAA_055590 {ECO:0000313|EMBL:EEA21763.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA21763.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995903; EEA21763.1; -; Genomic_DNA.
DR RefSeq; XP_002150372.1; XM_002150336.1.
DR AlphaFoldDB; B6QKY6; -.
DR STRING; 441960.B6QKY6; -.
DR VEuPathDB; FungiDB:PMAA_055590; -.
DR HOGENOM; CLU_016922_1_2_1; -.
DR OrthoDB; 1445768at2759; -.
DR PhylomeDB; B6QKY6; -.
DR Proteomes; UP000001294; 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:UP000001294}.
SQ SEQUENCE 438 AA; 47641 MW; BF0B5790147A4DEE CRC64;
MQPELVKELQ TALDAAKSRY IASNPRSNAF HEEAVNVMPG GNTRTILHTD PFPIYMKHGK
SYQVTSEDGI TYTDMAGEFT AALYGHSNPV ILSAMNDVLQ NVGMNIGATT AQERLFTSEI
CKRFQLERMR FTNSGTEANL HALAAARKFT GKRKVVTFSG GYHGAVLMFS GGRPASNNVD
MDDWIVVKYN DLDAAKEAIR SPGVAAVLVE GMQGANGSIC GTSEFLQGIQ QASSEVGVLF
ILDEVMTSRI SAGGLAALRG LKPDLKTFGK YLGGGLAFGS FGGRADVMAA FDPRLNGYIS
HSGTFNNNTL VTHVGHVGLT KVFTPEVARS FTEVGDKFRE KLNEVTKGTR IYFTGVGTVA
TAHFLAKGTR YIECADDVEE ISELRTLFWF EMLDAGFWVT LRGFIALILE TPPSELERFV
QAVQSFISKH QNLVALDA
//
