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Database: UniProt
Entry: S3CKC4_GLAL2
LinkDB: S3CKC4_GLAL2
Original site: S3CKC4_GLAL2 
ID   S3CKC4_GLAL2            Unreviewed;       520 AA.
AC   S3CKC4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   13-SEP-2023, entry version 44.
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=GLAREA_02886 {ECO:0000313|EMBL:EPE26972.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE26972.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE26972.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
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; KE145370; EPE26972.1; -; Genomic_DNA.
DR   RefSeq; XP_008086162.1; XM_008087971.1.
DR   AlphaFoldDB; S3CKC4; -.
DR   STRING; 1116229.S3CKC4; -.
DR   GeneID; 19461942; -.
DR   KEGG; glz:GLAREA_02886; -.
DR   eggNOG; KOG4513; Eukaryota.
DR   HOGENOM; CLU_026099_2_0_1; -.
DR   OrthoDB; 212at2759; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000016922; 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:UP000016922}.
FT   DOMAIN          6..506
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          87..299
FT                   /note="BPG-independent PGAM N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06415"
FT   ACT_SITE        67
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-1"
FT   BINDING         13
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         67
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         158..159
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         262..265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         336
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;  56874 MW;  58440FE257D1B845 CRC64;
     MTVDNKACLI VIDGWGIPSE SSPKNGDAIA AAETPVMDAF AKNADGYTEL EASSLAVGLP
     EGLMGNSEVG HLNIGAGRVV WQDVVRIDQT IKNNELNKNE VIMKVFNDAK SGNGRLHLCG
     LISDGGVHAK QDHLYALLKL AKEVGVPKVF IHFFGDGRDT DPKSGAGYMQ GLLDQIKQIG
     IGEIASVTGR YYAMDRDKRW ERVEVGLNAL CIGDGEESSD PVKTIKERYE KGENDEFLKP
     IIIGGKEARI SEGDQVFFFN YRSDRVREIT QLLGDADRSP LEDFAYPKNI TLTTMTQYKL
     DYPFPIAFKP QHMGNVLAET LGEQGVEQVH VAETEKYAHV TFFFNGGVEK SFPLETRDES
     QDLVPSNKSV ATYDLAPEMS AMGVAKQVSK RIAEGKFPFV MNNFAPPDMV GHTGVYEAAI
     VGVATTDKGI GEIYETCKKE GYLLFITSDH GNAEEMKFED GKPKTSHTTN KVPFVMANAP
     KGWSLKKTDG VLGDVAPTIL EAMGLKQPEE MTGKSLLVKS
//
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