ID Q1XF17_SORMA Unreviewed; 227 AA.
AC Q1XF17;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-independent) {ECO:0000256|ARBA:ARBA00012026};
DE EC=5.4.2.12 {ECO:0000256|ARBA:ARBA00012026};
DE Flags: Fragment;
GN Name=pgm {ECO:0000313|EMBL:CAJ14948.1};
OS Sordaria macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX NCBI_TaxID=5147 {ECO:0000313|EMBL:CAJ14948.1};
RN [1] {ECO:0000313|EMBL:CAJ14948.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S48977 {ECO:0000313|EMBL:CAJ14948.1};
RC TISSUE=Mycelium {ECO:0000313|EMBL:CAJ14948.1};
RX PubMed=16553871; DOI=10.1111/j.1574-6968.2006.00192.x;
RA Nowrousian M., Kuck U.;
RT "Comparative gene expression analysis of fruiting body development in two
RT filamentous fungi.";
RL FEMS Microbiol. Lett. 257:328-335(2006).
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; AM042545; CAJ14948.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1XF17; -.
DR VEuPathDB; FungiDB:SMAC_03693; -.
DR UniPathway; UPA00109; UER00186.
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 Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.40.1450.10; BPG-independent phosphoglycerate mutase, domain B; 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 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 SUPFAM; SSF64158; 2,3-Bisphosphoglycerate-independent phosphoglycerate mutase, substrate-binding domain; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 2..58
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT DOMAIN 59..227
FT /note="BPG-independent PGAM N-terminal"
FT /evidence="ECO:0000259|Pfam:PF06415"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAJ14948.1"
FT NON_TER 227
FT /evidence="ECO:0000313|EMBL:CAJ14948.1"
SQ SEQUENCE 227 AA; 24910 MW; B918F30D4F94DBF8 CRC64;
IAAAETPVMD ELSKSATGFT ELDASSLAVG LPEGLMGNSE VGHLNIGAGR VVWQDVVRID
QTIKKGELGQ NDVIKSTFER ARNGNGRLHL CGLISHGGVH AKQTHLYALL RAAKEAGVPK
IYIHFFGDGR DTDPKSGAGY MQELLDTIKE IGIGELATVV GRYYAMDRDK RWERVEVALK
GLYLGEGEES TDPVKTIKER YEKGENDEFL KPIIIGGDER RIKEDDT
//
