ID   PMM_CANAL               Reviewed;         252 AA.
AC   P31353; A0A1D8PCR5; Q5AIB6;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   13-SEP-2023, entry version 135.
DE   RecName: Full=Phosphomannomutase;
DE            Short=PMM;
DE            EC=5.4.2.8 {ECO:0000305|PubMed:1473182};
GN   Name=PMM1; OrderedLocusNames=CAALFM_C102480WA;
GN   ORFNames=CaO19.10454, CaO19.2937;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX   PubMed=1473182; DOI=10.1007/bf00326416;
RA   Smith D.J., Cooper M., De Tiani M., Losberger C., Payton M.A.;
RT   "The Candida albicans PMM1 gene encoding phosphomannomutase complements a
RT   Saccharomyces cerevisiae sec 53-6 mutation.";
RL   Curr. Genet. 22:501-503(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS.
RA   Stogios P.J.;
RT   "Crystal structure of the phosphomannomutase PMM1 from Candida albicans,
RT   apoenzyme state.";
RL   Submitted (DEC-2016) to the PDB data bank.
CC   -!- FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-
CC       phosphate-mannose required for a number of critical mannosyl transfer
CC       reactions.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC         Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC         EC=5.4.2.8; Evidence={ECO:0000305|PubMed:1473182};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC       step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR   EMBL; M96770; AAA34356.1; -; Genomic_DNA.
DR   EMBL; CP017623; AOW25932.1; -; Genomic_DNA.
DR   RefSeq; XP_721436.1; XM_716343.1.
DR   PDB; 5UE7; X-ray; 1.95 A; A/B=1-252.
DR   PDBsum; 5UE7; -.
DR   AlphaFoldDB; P31353; -.
DR   SMR; P31353; -.
DR   BioGRID; 1219946; 1.
DR   STRING; 237561.P31353; -.
DR   EnsemblFungi; C1_02480W_A-T; C1_02480W_A-T-p1; C1_02480W_A.
DR   GeneID; 3636852; -.
DR   KEGG; cal:CAALFM_C102480WA; -.
DR   CGD; CAL0000183926; PMM1.
DR   VEuPathDB; FungiDB:C1_02480W_A; -.
DR   eggNOG; KOG3189; Eukaryota.
DR   HOGENOM; CLU_065642_0_1_1; -.
DR   InParanoid; P31353; -.
DR   OMA; ISHRVYT; -.
DR   OrthoDB; 167037at2759; -.
DR   UniPathway; UPA00126; UER00424.
DR   PRO; PR:P31353; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004615; F:phosphomannomutase activity; IGI:CGD.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006013; P:mannose metabolic process; IBA:GO_Central.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   CDD; cd02585; HAD_PMM; 1.
DR   Gene3D; 3.30.1240.20; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR005002; PMM.
DR   InterPro; IPR043169; PMM_cap.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR10466:SF0; PHOSPHOMANNOMUTASE; 1.
DR   Pfam; PF03332; PMM; 1.
DR   SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR   SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   COMPLUYEAST-2DPAGE; P31353; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN           1..252
FT                   /note="Phosphomannomutase"
FT                   /id="PRO_0000199701"
FT   ACT_SITE        16
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   ACT_SITE        18
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         16
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:5UE7"
FT   BINDING         18
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:5UE7"
FT   BINDING         25
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         127
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         138
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         145
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         183
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         185
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000250|UniProtKB:Q92871"
FT   BINDING         213
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:5UE7"
FT   BINDING         225
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:5UE7"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:5UE7"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:5UE7"
FT   STRAND          11..17
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   TURN            18..20
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           30..42
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          43..48
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           53..60
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           91..95
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           97..113
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           142..155
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           157..168
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          174..179
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   TURN            180..182
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          183..188
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           193..199
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           201..203
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          206..213
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           222..225
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   STRAND          231..234
FT                   /evidence="ECO:0007829|PDB:5UE7"
FT   HELIX           238..248
FT                   /evidence="ECO:0007829|PDB:5UE7"
SQ   SEQUENCE   252 AA;  29019 MW;  25455FC315D85212 CRC64;
     MSFANKQDPK TLVLFDVDGT LTPARLTISE EMKKTLEKLR EKVVIGFVGG SDLSKQVEQL
     GPNVLNDFDY CFSENGLTAY KLGKELASQS FINWIGNEKY NKLVKFILRY LSDIDLPIRR
     GTFIEFRNGM INVSPIGRNA STQERNDYEK FDKQHHIRET MVEALKKEFP DFGLTYSIGG
     QISFDVFPTG WDKTYCLQHV EDEHFENIHF FGDKSYKGGN DYEIYNDPRT IGHAVNSPDD
     TIRILNETFK LQ
//