PMM_CANAL
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 03-AUG-2022, entry version 130.
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 COMPLUYEAST-2DPAGE; P31353; -.
DR PRIDE; P31353; -.
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; VCPIGRQ; -.
DR OrthoDB; 1038583at2759; -.
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; -; 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 PANTHER; PTHR10466; PTHR10466; 1.
DR Pfam; PF03332; PMM; 1.
DR SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
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
