GenomeNet

Database: UniProt
Entry: A0A165QAL1_EXIGL
LinkDB: A0A165QAL1_EXIGL
Original site: A0A165QAL1_EXIGL 
ID   A0A165QAL1_EXIGL        Unreviewed;       559 AA.
AC   A0A165QAL1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   13-SEP-2023, entry version 29.
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=EXIGLDRAFT_738068 {ECO:0000313|EMBL:KZW03328.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW03328.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW03328.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW03328.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KV425884; KZW03328.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165QAL1; -.
DR   STRING; 1314781.A0A165QAL1; -.
DR   InParanoid; A0A165QAL1; -.
DR   OrthoDB; 212at2759; -.
DR   UniPathway; UPA00109; UER00186.
DR   Proteomes; UP000077266; 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:UP000077266}.
FT   DOMAIN          8..544
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
FT   DOMAIN          87..329
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         15
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         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         294..297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         366
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-2"
FT   BINDING         433
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         437
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         474
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         475
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
FT   BINDING         492
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001492-3"
SQ   SEQUENCE   559 AA;  61651 MW;  B73677CC1A74FA41 CRC64;
     MPAKVANKVC LIVHDGWGIS DAPPEKGNAV AAGSTVNMDS IAEKHSYRKL AAHGLAVGLN
     DGLMGNSEVG HLNIGAGRIV WQDIVKIDQS IKKRQFHKNE TILESFKHAK DSTGRLHLIG
     LVSDGGVHSH ITHLYALIET AREVGVPHVF VHFIGDGRDT DPKSAVTYMR QLLDFIAKDS
     EQHKDTKVEI ATVVGRYYAM DRDKRWDRVK LAIDGLVQGT GENIETIEVA KDGKGDELVK
     KIEERYAKDE KDEFLKPIVV KGDGRVKGES FSPHSLLLLS HEPDKDTIFF FNYRSDRMRE
     IASVFGIDPK PMEVTVPKDI HITTMSRYNV EFPFKIAYPP QAMTNVLAET LSKQGVKQAH
     IAETEKYAHV TFFFNGGVEK QFEAEERHMI SSPKVATYDL QPEMSAQGVA DKVAEVVRAG
     THEFIMCNFA PPDMVGHTGM YDAAVKAISA TDKAVKTVYD ACEEAGYILL ITADHGNAEQ
     MQNPEGKPHT AHTTNPVPFI LTGGKDKWSL KEDTKGLGVS DDVDAEVGAL CDVAPTILDI
     MGLEIPKEMS GRSLLERKK
//
DBGET integrated database retrieval system