ID U7PMX3_SPOS1 Unreviewed; 663 AA.
AC U7PMX3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 08-NOV-2023, entry version 27.
DE RecName: Full=Phosphoglycerate mutase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1624_07205 {ECO:0000313|EMBL:ERS96296.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS96296.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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DR EMBL; KI440850; ERS96296.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PMX3; -.
DR STRING; 1391915.U7PMX3; -.
DR eggNOG; ENOG502RXMD; Eukaryota.
DR HOGENOM; CLU_015562_1_0_1; -.
DR OrthoDB; 118474at2759; -.
DR Proteomes; UP000018087; 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; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR46192; BROAD-RANGE ACID PHOSPHATASE DET1; 1.
DR PANTHER; PTHR46192:SF11; BROAD-RANGE ACID PHOSPHATASE DET1; 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 Reference proteome {ECO:0000313|Proteomes:UP000018087}.
FT REGION 238..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 12
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 105
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 11..18
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 663 AA; 72882 MW; DDF9452CAEDBB9B0 CRC64;
MGKPRLLIIV RHGQSEGNKN RDIHQTIPDH RVRLTHEGWQ QAYDAGRRLR ALLRADDTIQ
VFTSPYRRTR ETTEGILQTL TSDDPEPSPF KRNNIKVYEE PRLREQDFGN FQPCSAEMER
MWQERADYGH FFYRIPNGES AADAYDRVSG FNESLWRQFG EDDFPSVCVL VTHGLMSRVF
LMKWYHFSVE YFEDLRNVNH CEFLIMRKQG DSGKYKLESK LRTWSELRRE RAALLKQKEE
LASKEKSEKG DKDSAKLERA ESGLSSPSST ALVPQRRWGG CPNGCNHDKN FKIRPGLADL
ILRDGTNVYD NANGSPRASK STSAINNHGH GKSSGTPPSL SRRTTAVRRF QVAGYSDDDD
GGDGGDEVDD DNRPSSQASN DTSNDASSKS AMHAANATGS GSGAAGGLAP PHIDITRARE
EIVSSPDATP SFITPEDRQR VVSPGSSPPP MPKSLLHIGR DFGGTYSGHT SDADSSEDDR
VRHRMAHLKL HAGSSTESGA QYTRSHSHGH GHNYYGSHSS DRFVYGTLDA VAASATMPRS
GTSKTEAAAA VSTLQGGPMS AGSAGGGSSN LSNIRKKRTK NMANRLGDAP YCSDCDHDHD
HDHDHDHDHG DTTDVGADEL HATDELLNAD VVLIDSNGDD ATDVDPDMAQ AERDDKSIQG
SVY
//
