GenomeNet

Database: UniProt
Entry: B6QB14_TALMQ
LinkDB: B6QB14_TALMQ
Original site: B6QB14_TALMQ 
ID   B6QB14_TALMQ            Unreviewed;       328 AA.
AC   B6QB14;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Carboxyphosphonoenolpyruvate phosphonomutase, putative {ECO:0000313|EMBL:EEA25355.1};
GN   ORFNames=PMAA_064670 {ECO:0000313|EMBL:EEA25355.1};
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:EEA25355.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate +
CC         succinate; Xref=Rhea:RHEA:16809, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57429; EC=4.1.3.30;
CC         Evidence={ECO:0000256|ARBA:ARBA00001050};
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DR   EMBL; DS995900; EEA25355.1; -; Genomic_DNA.
DR   RefSeq; XP_002145902.1; XM_002145866.1.
DR   AlphaFoldDB; B6QB14; -.
DR   STRING; 441960.B6QB14; -.
DR   VEuPathDB; FungiDB:PMAA_064670; -.
DR   HOGENOM; CLU_027389_3_0_1; -.
DR   OrthoDB; 554215at2759; -.
DR   PhylomeDB; B6QB14; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   CDD; cd00377; ICL_PEPM; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   InterPro; IPR039556; ICL/PEPM.
DR   InterPro; IPR018523; Isocitrate_lyase_ph_CS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR42905:SF2; PHOSPHOENOLPYRUVATE CARBOXYLASE FAMILY PROTEIN; 1.
DR   Pfam; PF13714; PEP_mutase; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00161; ISOCITRATE_LYASE; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyruvate {ECO:0000313|EMBL:EEA25355.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001294}.
SQ   SEQUENCE   328 AA;  35081 MW;  6FE54226686CA98D CRC64;
     MAITITLGPN GQYQVNGAAN GLDHNLDLVP ISGATKLRRM LNETDELIVC PGVYDGLSAR
     IAMQLGFSAM YMTGAGTTAS RLGMADLGLA QLHDMKTNAE MIAGLDPYGP PLIADMDTGY
     GGPLMVAKSV QQYIQAGVAG FHIEDQVLSK RCGHLAGKKV VSKEEYLMRI RAAKSTIDRL
     HSDIVLIART DALQQYGYEE CIDRLKAARD LGADVGLLEG FTSKEQARQA VQDLAPWPVL
     LNMVENGAGP VITTFEAKEM GFRINIFSFA SLAPAYLGIR AALERLKTDG VTGIPDGLGP
     RKLFEICGLS ESMKIDAEAG NSAFVNGV
//
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