MPI_OGAPD
ID MPI_OGAPD Reviewed; 426 AA.
AC Q8J093; E7R1T0; W1QIL2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=PMI40; ORFNames=HPODL_00814;
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1;
RX PubMed=12112240; DOI=10.1002/yea.881;
RA Kim M.W., Agaphonov M.O., Kim J.Y., Rhee S.K., Kang H.A.;
RT "Sequencing and functional analysis of the Hansenula polymorpha genomic
RT fragment containing the YPT1 and PMI40 genes.";
RL Yeast 19:863-871(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1;
RA Kim M.W., Agaphonov M.O., Rhee S.K., Kang H.A.;
RT "Molecular cloning of the Hansenula polymorpha homolog of the Saccharomyces
RT cerevisiae PMI40 gene.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1;
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
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; AF454544; AAN52529.1; -; Genomic_DNA.
DR EMBL; AF346819; AAN64443.1; -; Genomic_DNA.
DR EMBL; AEOI02000005; ESX01420.1; -; Genomic_DNA.
DR RefSeq; XP_013936254.1; XM_014080779.1.
DR AlphaFoldDB; Q8J093; -.
DR SMR; Q8J093; -.
DR STRING; 1005962.Q8J093; -.
DR EnsemblFungi; ESX01420; ESX01420; HPODL_00814.
DR GeneID; 25770283; -.
DR eggNOG; KOG2757; Eukaryota.
DR HOGENOM; CLU_026967_0_0_1; -.
DR OMA; DIGLFCG; -.
DR OrthoDB; 1043197at2759; -.
DR UniPathway; UPA00126; UER00423.
DR Proteomes; UP000008673; Chromosome III.
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:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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..426
FT /note="Mannose-6-phosphate isomerase"
FT /id="PRO_0000194246"
FT ACT_SITE 296
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 426 AA; 46779 MW; 8247706E7BECEE35 CRC64;
MSSAPKLFRV IGGAQNYDWG KLGSTSAVAR FAKLNDPENV SIEEEKPYAE LWMGTHPSVP
TVSAQDRTPL RDLVRAAPEE MLGQDIIDKF GSKEGIPFLF KVLSIRKVLS IQAHPDKALA
RQLHASDPKH YPDDNHKPEM AVAITDFEAF CGFKPLAEID ALLQKIPEFR ELVGDDVVAE
FHSGIDSSDV AGKKKLLQKV FSRVMNSPES KFEPLAARLV ERTKSDPQLF GETLADLIQR
LDAQFPNDIG LFCGCLLLNH CILKSGEAMF LEAKDPHAYI SGDIMECMAA SDNVIRAGFT
PKFKDVEVLV DCLTYSFNPV EEQKLKPAPF PRGTGVAELK LYDPPIDEFS VLQTTFTSAG
AEKFEGLDGP SLLIVTEGKG KIKLQGSDEA LDASTGNIFF VAPKAAIELV SESKDTFTSY
RAFCEA
