MPI_CANAL
ID MPI_CANAL Reviewed; 441 AA.
AC P34948; A0A1D8PII7; Q59YD6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Mannose-6-phosphate isomerase;
DE EC=5.3.1.8 {ECO:0000269|PubMed:8180205};
DE AltName: Full=Phosphohexomutase;
DE AltName: Full=Phosphomannose isomerase;
DE Short=PMI;
GN Name=PMI1; Synonyms=MANA; OrderedLocusNames=CAALFM_C209640WA;
GN ORFNames=CaO19.1390;
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].
RC STRAIN=1006;
RX PubMed=7785330; DOI=10.1002/yea.320110402;
RA Smith D.J., Proudfoot A.E.I., de Tiani M., Wells T.N.C., Payton M.A.;
RT "Cloning and heterologous expression of the Candida albicans gene PMI 1
RT encoding phosphomannose isomerase.";
RL Yeast 11:301-310(1995).
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 CHEMICAL LABELLING OF CYS-150, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8260497; DOI=10.1021/bi00214a010;
RA Coulin F., Magnenat E., Proudfoot A.E.I., Payton M.A., Scully P.,
RA Wells T.N.C.;
RT "Identification of Cys-150 in the active site of phosphomannose isomerase
RT from Candida albicans.";
RL Biochemistry 32:14139-14144(1993).
RN [6]
RP ACTIVE SITE ARG-304, PROTEIN SEQUENCE OF 300-312, AND CATALYTIC ACTIVITY.
RX PubMed=8180205; DOI=10.1021/bi00185a015;
RA Wells T.N.C., Scully P., Magnenat E.;
RT "Arginine 304 is an active site residue in phosphomannose isomerase from
RT Candida albicans.";
RL Biochemistry 33:5777-5782(1994).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=8612079; DOI=10.1038/nsb0596-470;
RA Cleasby A., Wonacott A., Skarzynski T., Hubbard R.E., Davies G.J.,
RA Proudfoot A.E.I., Bernard A.R., Payton M.A., Wells T.N.C.;
RT "The X-ray crystal structure of phosphomannose isomerase from Candida
RT albicans at 1.7-A resolution.";
RL Nat. Struct. Biol. 3:470-479(1996).
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=D-mannose 6-phosphate = D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:12356, ChEBI:CHEBI:58735, ChEBI:CHEBI:61527;
CC EC=5.3.1.8; Evidence={ECO:0000269|PubMed:8180205};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC step 1/2.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X82024; CAA57548.1; -; Genomic_DNA.
DR EMBL; CP017624; AOW27942.1; -; Genomic_DNA.
DR PIR; S55354; S55354.
DR RefSeq; XP_714562.1; XM_709469.1.
DR PDB; 1PMI; X-ray; 1.70 A; A=2-441.
DR PDB; 5NW7; X-ray; 1.85 A; A=1-441.
DR PDBsum; 1PMI; -.
DR PDBsum; 5NW7; -.
DR AlphaFoldDB; P34948; -.
DR SMR; P34948; -.
DR STRING; 237561.P34948; -.
DR BindingDB; P34948; -.
DR ChEMBL; CHEMBL3946; -.
DR GeneID; 3643795; -.
DR KEGG; cal:CAALFM_C209640WA; -.
DR CGD; CAL0000189115; PMI1.
DR VEuPathDB; FungiDB:C2_09640W_A; -.
DR eggNOG; KOG2757; Eukaryota.
DR HOGENOM; CLU_026967_0_0_1; -.
DR InParanoid; P34948; -.
DR OrthoDB; 1043197at2759; -.
DR BRENDA; 5.3.1.8; 1096.
DR UniPathway; UPA00126; UER00423.
DR EvolutionaryTrace; P34948; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IDA:CGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IEA:EnsemblFungi.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR001250; Man6P_Isoase-1.
DR InterPro; IPR016305; Mannose-6-P_Isomerase.
DR InterPro; IPR018050; Pmannose_isomerase-type1_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR PANTHER; PTHR10309; PTHR10309; 1.
DR Pfam; PF01238; PMI_typeI; 1.
DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1.
DR PRINTS; PR00714; MAN6PISMRASE.
DR SUPFAM; SSF51182; SSF51182; 1.
DR TIGRFAMs; TIGR00218; manA; 1.
DR PROSITE; PS00965; PMI_I_1; 1.
DR PROSITE; PS00966; PMI_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isomerase;
KW Metal-binding; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..441
FT /note="Mannose-6-phosphate isomerase"
FT /id="PRO_0000194241"
FT ACT_SITE 304
FT /evidence="ECO:0000269|PubMed:8180205"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT SITE 150
FT /note="Its modification inactivates the enzyme"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1PMI"
FT TURN 62..66
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:1PMI"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 155..164
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 193..210
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 214..230
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 258..261
FT /evidence="ECO:0007829|PDB:1PMI"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 285..298
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:1PMI"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:1PMI"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 382..395
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 398..406
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:1PMI"
FT STRAND 433..438
FT /evidence="ECO:0007829|PDB:1PMI"
SQ SEQUENCE 441 AA; 48867 MW; AEDDE2AE9EDAD5EC CRC64;
MSSEKLFRIQ CGYQNYDWGK IGSSSAVAQF VHNSDPSITI DETKPYAELW MGTHPSVPSK
AIDLNNQTLR DLVTAKPQEY LGESIITKFG SSKELPFLFK VLSIEKVLSI QAHPDKKLGA
QLHAADPKNY PDDNHKPEMA IAVTDFEGFC GFKPLDQLAK TLATVPELNE IIGQELVDEF
ISGIKLPAEV GSQDDVNNRK LLQKVFGKLM NTDDDVIKQQ TAKLLERTDR EPQVFKDIDS
RLPELIQRLN KQFPNDIGLF CGCLLLNHVG LNKGEAMFLQ AKDPHAYISG DIIECMAASD
NVVRAGFTPK FKDVKNLVEM LTYSYESVEK QKMPLQEFPR SKGDAVKSVL YDPPIAEFSV
LQTIFDKSKG GKQVIEGLNG PSIVIATNGK GTIQITGDDS TKQKIDTGYV FFVAPGSSIE
LTADSANQDQ DFTTYRAFVE A
