ID A0A0F4GSQ6_9PEZI Unreviewed; 521 AA.
AC A0A0F4GSQ6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 13-SEP-2023, entry version 31.
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=TI39_contig336g00050 {ECO:0000313|EMBL:KJY00284.1};
OS Zymoseptoria brevis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY00284.1, ECO:0000313|Proteomes:UP000033647};
RN [1] {ECO:0000313|EMBL:KJY00284.1, ECO:0000313|Proteomes:UP000033647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zb18110 {ECO:0000313|EMBL:KJY00284.1,
RC ECO:0000313|Proteomes:UP000033647};
RA Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT "RNA-seq based gene annotation and comparative genomics of four
RT Zymoseptoria species reveal species-specific pathogenicity related genes
RT and transposable element activity.";
RL Submitted (MAR-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}.
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:KJY00284.1}.
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DR EMBL; LAFY01000328; KJY00284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4GSQ6; -.
DR STRING; 1047168.A0A0F4GSQ6; -.
DR OrthoDB; 212at2759; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000033647; 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:UP000033647}.
FT DOMAIN 7..507
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 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 521 AA; 57265 MW; C9DC6AFB63C6ED37 CRC64;
MVQVKQKAAL ICIDGWGIPV ISSDPKGNAI LNAETPWMDE FATEGSKITS GYTELEASSL
AVGLPEGLMG NSEVGHLNIG AGRVVWQDVV RIDQTIKKGE MNKVENIVKS FTRAKEGNGR
LHLCGLVSDG GVHSHINHLK ELLKVAKEIG VPEVYIHFFG DGRDTDPKSG KGHLEDLLAF
TKEQSIGKLA TIVGRYYVMD RDKRWERVEL GLKGMVTGEG EESSDPVGTF QARYDAGEND
EFLKPIIING KEGRISDKDT VFFFNYRSDR VREVVQLLGD QDRSPRPDFP YPSDIHLTTM
TRYKTDFNLP IAFAPVSMDN VLADWLGQHD VKQVHIAETE KFAHVTFFFN GGQETQYPGE
DRDLIPSPKG VATYDLEPKM SAMGVAGKMA ERIAAGEHEF IMNNFAPPDM VGHTGVYDAA
VIACGETDKA IGVVYEACKK HGYTLFITAD HGNAEEMLTE EKTPKTSHTT NKVPFVMANA
PEGWSLKRTD GVLGDVAPTV LACMGLEQPK EMTGTSLLVK K
//
