ID A0A364L835_9EURO Unreviewed; 295 AA.
AC A0A364L835;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Phosphonopyruvate hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BHQ10_007987 {ECO:0000313|EMBL:RAO71975.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO71975.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO71975.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO71975.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily. PEP
CC mutase family. {ECO:0000256|ARBA:ARBA00038455}.
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:RAO71975.1}.
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DR EMBL; MIKG01000017; RAO71975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364L835; -.
DR STRING; 1196081.A0A364L835; -.
DR OrthoDB; 2678353at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd00377; ICL_PEPM; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR039556; ICL/PEPM.
DR InterPro; IPR012649; PPH.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR02321; Pphn_pyruv_hyd; 1.
DR PANTHER; PTHR42905; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR42905:SF7; PHOSPHOENOLPYRUVATE PHOSPHOMUTASE-RELATED; 1.
DR Pfam; PF13714; PEP_mutase; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000249363}.
SQ SEQUENCE 295 AA; 31666 MW; 96D9A170AB4433AC CRC64;
MARQASAVAL RKLLNKSKPA IAMASHNPLS ANLAAEAGFN AIWVSGFELS ASYAVPDASL
LPMSTHLEMT RSIAESLADK SFPLVVDVDT GFGNAINVAY IIPRFEAAGA AAVVIEDKHF
PKDSSLRTNG RQVLVTIEEF QGKIAAAKAK SDSMLIIART EALIAGLGQE EAQRRALAYV
EAGADAILIH SKQLTPEEIL SFCRSWPDEQ VPLVLVPTSY PQLSFTDITA LGKVGLIICG
NHAIRASVAS MRNVFGRILK DDGLAGVEED IASVSEIFEL QGDSAMRKLE KDYLR
//
