GenomeNet

Database: UniProt
Entry: M9LT60_PSEA3
LinkDB: M9LT60_PSEA3
Original site: M9LT60_PSEA3 
ID   M9LT60_PSEA3            Unreviewed;       997 AA.
AC   M9LT60;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:GAC71689.1};
GN   ORFNames=PANT_5c00025 {ECO:0000313|EMBL:GAC71689.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC71689.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; DF196771; GAC71689.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9LT60; -.
DR   STRING; 1151754.M9LT60; -.
DR   OrthoDB; 9136at2759; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR013745; Bit61/PRR5.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR   PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR   Pfam; PF08539; HbrB; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976}.
FT   REGION          302..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          374..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          804..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          924..997
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        925..945
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        973..997
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        13
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        90
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         12..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   997 AA;  103538 MW;  9C2DFD5921E612D5 CRC64;
     MSLNRLLVTL VRHGESQDNS MGIWAGFRDT PLTQNGINQA RALGQSFANV PLTAIYCSDL
     KRAAMTADEI LKSNRSIPPP PLVQSKTLRE INFGQAEGQT NTHTEWIQGS TGEDGRKFRF
     PQGECLEEVN ARIAKAVRQF ILPRVEALRK KPPTQQHAAG DLGHICIVAH GIAIAELLRV
     FMSLHDGSPN SPWPDPKLSY QRVRLENTGW SRLELAVPFQ GDDTSPVEPH PTPLKTSFAH
     YADFGGTAND LSEASTDAQG RPVLHHDLAS PSLHVSRSGL GGPEAAARPI YVKILCQNQT
     DHLHGSTAQP SSMSSAAKAV AHLAGGGASK PAPASNPAQG SALAQPTSAG ATSSAAVGLP
     SSATLASIAS NATSSHSHST AAMTPSTPAA GAFQATNGTS KNSTTTPASA RNLLAYDARM
     MTRELERAGA TAMLSGSEAG ASGAMGSSYY PSSGSTSTLA ADRTASSVGL GAAAANASIG
     GTERSAFNTS PAVGSALNSS AGASQSGTSG QQASTLFGSY PQTGSASVPG AASPNPGALS
     FNVGPSISSD TWQMICIRVL PLFNGEPLRT SIEELNEMVT LHIRKTLERS QTHAIESLTL
     DLLSLTSTGT LTLNSKLQGL DDQRLLLRLV EVWTFFLGQV LPYCEGCFLP LRTDPALRNL
     VATSGSYGAA NGTAGIATSS SSAGLFSAGS NLTQSGAALL LSGAPSTGMD LQLIDVRKVL
     MVVFRDQVLM PIYERLFQLF AHLTDLDPAF AAGEDAHAAG GGDDGIKQVS LRLLQMTSVL
     AGILSEDQAQ EAMDNLLRAL RLGSKSPSAG RSGVAGDAPG ARSASPSQRH NRRGWMAQKA
     RKHGVTSNGE TDIDRSLSGL SLGPGQSAGK GFAHAMQAGP DGHAHSAQHA FLKRPSQLTN
     FRDPLGSRYG PAMTEDEYLT SLRSPAGSPA ISTPGQPQTP AIPSTEGAVA SVDHAFERSQ
     HEDGGAVTPV SGRATSPAIN QIPRQSEQPS TAPALAA
//
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