MPI_CANGA
ID MPI_CANGA Reviewed; 429 AA.
AC Q76IQ2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mannose-6-phosphate isomerase;
DE EC=5.3.1.8;
DE AltName: Full=Phosphohexomutase;
DE AltName: Full=Phosphomannose isomerase;
DE Short=PMI;
GN Name=PMI1; Synonyms=PMI40; OrderedLocusNames=CAGL0J02244g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RA Nakayama H., Ohta A., Arisawa M., Sudoh M.;
RT "Isolation of the Candida glabrata PMI1 encoding phosphomannose isomerase
RT gene.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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. {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB097082; BAD02470.1; -; Genomic_DNA.
DR EMBL; CR380956; CAG60751.1; -; Genomic_DNA.
DR RefSeq; XP_447802.1; XM_447802.1.
DR AlphaFoldDB; Q76IQ2; -.
DR SMR; Q76IQ2; -.
DR STRING; 5478.XP_447802.1; -.
DR EnsemblFungi; CAG60751; CAG60751; CAGL0J02244g.
DR GeneID; 2889794; -.
DR KEGG; cgr:CAGL0J02244g; -.
DR CGD; CAL0133206; CAGL0J02244g.
DR VEuPathDB; FungiDB:CAGL0J02244g; -.
DR eggNOG; KOG2757; Eukaryota.
DR HOGENOM; CLU_026967_0_0_1; -.
DR InParanoid; Q76IQ2; -.
DR OMA; DIGLFCG; -.
DR UniPathway; UPA00126; UER00423.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
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:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
KW Cytoplasm; Isomerase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..429
FT /note="Mannose-6-phosphate isomerase"
FT /id="PRO_0000194242"
FT ACT_SITE 301
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 429 AA; 47589 MW; BC444CC3F9A89FE7 CRC64;
MTSDRFFRLD AGYQQYDWGK IGSSSAVAKF AAHSDPSVKI DETKPYAELW MGTHSKLPSV
NHETKATLND ILAKNSQELI GEDVINKFKS TNELPFLFKV LSIEKVLSIQ AHPDKELGKK
LHMEDPKNYP DDNHKPEMAV AITEFEGFCG FKPLEEIADE LETIPEFRDV VGDEVANEFI
QNYKTGVENS SSACANNKKL LQKVFEKVMT APCDILEKNA DGMAKRANEN PSSFKSSDLP
ELVVRLNRQF PKDVGLFCGC LMLNHCKLQP GQALFLEAKD PHAYICGDII ECMAASDNVV
RAGFTPKFKD VKNLVEMLTY RYDPVEKQVM SAEEFPRAGG DGATIMYNPP IAEFSVLETT
FKNKTGKATV EGLKGPSIVI TTAGEGYISA DGQKLKAEPG FVFFIGANVP VELETTDKDF
TTYRAFVEA
