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Database: UniProt
Entry: A0A094EG62_9PEZI
LinkDB: A0A094EG62_9PEZI
Original site: A0A094EG62_9PEZI 
ID   A0A094EG62_9PEZI        Unreviewed;       522 AA.
AC   A0A094EG62;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE            EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
GN   ORFNames=V499_04633 {ECO:0000313|EMBL:KFY75378.1};
OS   Pseudogymnoascus sp. VKM F-103.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY75378.1, ECO:0000313|Proteomes:UP000029295};
RN   [1] {ECO:0000313|EMBL:KFY75378.1, ECO:0000313|Proteomes:UP000029295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY75378.1,
RC   ECO:0000313|Proteomes:UP000029295};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798}.
CC   -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC       family. {ECO:0000256|ARBA:ARBA00008819}.
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:KFY75378.1}.
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DR   EMBL; JPKB01000709; KFY75378.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094EG62; -.
DR   HOGENOM; CLU_026099_2_0_1; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000029295; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16010; iPGM; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 1.
DR   HAMAP; MF_01038; GpmI; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR011258; BPG-indep_PGM_N.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR036646; PGAM_B_sf.
DR   InterPro; IPR005995; Pgm_bpd_ind.
DR   NCBIfam; TIGR01307; pgm_bpd_ind; 1.
DR   PANTHER; PTHR31637; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   PANTHER; PTHR31637:SF0; 2,3-BISPHOSPHOGLYCERATE-INDEPENDENT PHOSPHOGLYCERATE MUTASE; 1.
DR   Pfam; PF06415; iPGM_N; 1.
DR   Pfam; PF01676; Metalloenzyme; 1.
DR   PIRSF; PIRSF001492; IPGAM; 1.
DR   SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR001492-3};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001492-3}.
FT   DOMAIN          6..508
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          88..300
FT                   /note="BPG-independent PGAM N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06415"
FT   ACT_SITE        68
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-1"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         68
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         159..160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         263..266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         337
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         409
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         413
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         450
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         451
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         468
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
SQ   SEQUENCE   522 AA;  57765 MW;  C1B2E0B727437D49 CRC64;
     MSKVDQKAVL IVIDGWGIPS ESSPKDGDAI TNANTPVMDE FYKNADGFIG LEASSLAVGL
     PEGLMGNSEV GHLNIGAGRV VWQDVVRIDQ TIRNNELDKN EIIMKTFQDA KNGTGRLHLC
     GLISDGGVHS KQDHLYALLK VAKEVGIPHV YIHFFGDGRD TDPKSGAGYM QQLVDKTKEI
     GIGEIATVVG RYYAMDRDKR WDRVEVALKG MVLGEGEDSS DPVATVKERY SKDENDEFLK
     PIIVGGKERR IQDNDEVFFF NYRSDRVREI TQLLGDVDRS PKPDFAYPKN IRLTTMTQYK
     LDYPFTIAFK PQHMGMVLAE TLGAQGVKQV HIAETEKYAH VTFFFNGGVE KVFPLEERDE
     SQDLVPSNKT VATYDLAPEM SAAGVAKQVS KRIQEQEYPF VMNNFAPPDM VGHTGVYEAA
     IKGVEATDKA IGEIYETCKR ENYVLFITSD HGNAEEMKFA DGKPKTSHTT NKVPFIMANA
     PKGWSLKATE DGVLGDVAPT ILEVMGLSQP EEMTGHSLLV KS
//
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