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Database: UniProt
Entry: Q2UKU9_ASPOR
LinkDB: Q2UKU9_ASPOR
Original site: Q2UKU9_ASPOR 
ID   Q2UKU9_ASPOR            Unreviewed;       570 AA.
AC   Q2UKU9;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=Glutamate decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AO090003000666 {ECO:0000313|EMBL:BAE57816.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE57816.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE57816.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
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DR   EMBL; AP007155; BAE57816.1; -; Genomic_DNA.
DR   RefSeq; XP_001819818.1; XM_001819766.1.
DR   AlphaFoldDB; Q2UKU9; -.
DR   STRING; 510516.Q2UKU9; -.
DR   EnsemblFungi; BAE57816; BAE57816; AO090003000666.
DR   GeneID; 5991801; -.
DR   KEGG; aor:AO090003000666; -.
DR   VEuPathDB; FungiDB:AO090003000666; -.
DR   HOGENOM; CLU_011856_0_0_1; -.
DR   OMA; RHATYHA; -.
DR   OrthoDB; 888358at2759; -.
DR   Proteomes; UP000006564; Chromosome 2.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.170; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT   MOD_RES         325
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   570 AA;  61819 MW;  DB7214EB18127772 CRC64;
     MAVSPPSRRA EEVRSLLSAV EDLLIPFIRS ADEDPLGQKA LENGVNGANG THNDLKPSGT
     SLVDHKKPEE LQSILQLELP EQGTGQDGLV EALQKVLRYS VNTWHQGFLD KLYASTNAPG
     VASELILAAL NTNVHVYQVS PALTVIEKFT GKQLASLFGL KGPRAGGISV QGGSASNTTS
     IVIARNNLFP ATKRDGNGDY RFVLFTSAHG HYSIEKAAQM LGLGSSSVWS VPIDKQGRMI
     PAELENLVRK ALKENRTPFY VNATAGTTVM GSFDPFDEIA AICKKYNLWF HVDGSWGGSF
     VFSKRQRQKL AGAEKADSIA INPHKMLGVP VTCSFLLAAD LRRFHRANTL PAGYLFHNED
     TELPEANGCN GAVESELSVD SPEVWDLADL TLQCGRRADS LKLFLGWTYY GTAGYEKQID
     AACDIAAHLA TLVAENPNFI LVSENPPPCL QVCFYYAPGG QFLHPRGVVS DEAERGKANS
     KVTEQVTHAI VSKGFMVDFA PPSGDDDVVG NGKFFRCVVN VQTTKETVEA LLQAIEEVGP
     GIVENMKVQK AQRKFNRPGE RGHGPVVHHP
//
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