ID A0A0D2G310_9EURO Unreviewed; 520 AA.
AC A0A0D2G310;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 36.
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=Z517_11930 {ECO:0000313|EMBL:KIW75158.1};
OS Fonsecaea pedrosoi CBS 271.37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW75158.1, ECO:0000313|Proteomes:UP000053029};
RN [1] {ECO:0000313|EMBL:KIW75158.1, ECO:0000313|Proteomes:UP000053029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW75158.1,
RC ECO:0000313|Proteomes:UP000053029};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL Submitted (JAN-2015) 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}.
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DR EMBL; KN846976; KIW75158.1; -; Genomic_DNA.
DR RefSeq; XP_013278966.1; XM_013423512.1.
DR AlphaFoldDB; A0A0D2G310; -.
DR STRING; 1442368.A0A0D2G310; -.
DR GeneID; 25311420; -.
DR VEuPathDB; FungiDB:Z517_11930; -.
DR HOGENOM; CLU_026099_2_0_1; -.
DR OrthoDB; 212at2759; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000053029; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053029}.
FT DOMAIN 7..506
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 92..304
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT ACT_SITE 72
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 72
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 163..164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 267..270
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 341
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT BINDING 408
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 412
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT BINDING 449
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
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 467
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
SQ SEQUENCE 520 AA; 57135 MW; B74BB6FFE6209A62 CRC64;
MTKVEHKAVL IVIDGWGIPS ESSPPEGDAI AAAETPFMDG FAKDGSTTAQ GYTELEASSL
AVGLPEGLMG NSEVGHLNIG AGRVVWQDVV RIDQTIKKGE MNKVANIQKC FKHAVDGNGR
LHLLGLISDG GVHSHINHLF ALLQVAKEMK VPKVFIHFFG DGRDTDPKSA AGYLQQLLDK
LKELGIGELA TVVGRYYIMD RDKRWDRVEI GMKGIVLGEG EESSDPVATI KARYEKGEND
EFLKPIIVGG DERRIKDNDT LFFFNYRSDR VREITQLLGD VDRSPKPDFP YPKGIEITTM
TQYKTDYPFP IAFPPQHMGN VLAEWLGKKG LKQCHVAETE KYAHVTFFFN GGVEKQFDGE
DRELIPSPKV ATYDLDPPMS AQKVADKLSE RIADQKYDFL MNNFAPPDMV GHTGVYEAAI
KGVTATDAAI GTVYEACKKN GYILFVTADH GNAEEMLNEE GKPKTSHTTN KVPFVMANAP
EGWSLKKQDG VLGDVAPTVL AAMGLDQPEE MSGTSLLVKK
//
