ID G2YD15_BOTF4 Unreviewed; 352 AA.
AC G2YD15;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Phosphoglycerate mutase family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BofuT4_P093710.1 {ECO:0000313|EMBL:CCD49663.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD49663.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; FQ790321; CCD49663.1; -; Genomic_DNA.
DR AlphaFoldDB; G2YD15; -.
DR STRING; 999810.G2YD15; -.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_033323_0_1_1; -.
DR InParanoid; G2YD15; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 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:UP000008177}.
FT ACT_SITE 61
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 138
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 60..67
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 110
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 352 AA; 39937 MW; AF3ED02624B72297 CRC64;
MTKQTRQIKF YIFFSTIKCF CLHNDHKHTQ LCTIQQSWQY SVNDHFFPLP YGGMRLLLIR
HGETVDNVAN VYAGVTDSAL TNHGVLQANR LGTHLAASKV SHIFSSDLQR AIKTAEAIRV
AQNNDPSFEV TKLELLREQD FGHYEKKPFH ERSKDSIKTA KEVHSQAHRI DPGFKDVESK
ESMKRRMETF VNKHLIHFLN IDENNLNDHT IAIVAHGIIL NHLWRVILRR FDPKNVSISP
NVPRPERGLE YLGGWSNTGY LDLDIKPIQE VTPSKVGSVP SVLDELSNAQ TSVMPPSHAV
DGAEVTMSLM IKSVNNIDHL KGLKKTRGGL GSLKHDSTQR TMDSFFKKRK LG
//