ID A5DFT3_PICGU Unreviewed; 429 AA.
AC A5DFT3;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 2.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Mannose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00018236, ECO:0000256|RuleBase:RU000611};
DE EC=5.3.1.8 {ECO:0000256|ARBA:ARBA00011956, ECO:0000256|RuleBase:RU000611};
GN ORFNames=PGUG_02134 {ECO:0000313|EMBL:EDK38036.2};
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746 {ECO:0000313|EMBL:EDK38036.2, ECO:0000313|Proteomes:UP000001997};
RN [1] {ECO:0000313|EMBL:EDK38036.2, ECO:0000313|Proteomes:UP000001997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL
RC Y-324 {ECO:0000313|Proteomes:UP000001997};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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:0000256|ARBA:ARBA00002564}.
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:0000256|ARBA:ARBA00000757,
CC ECO:0000256|RuleBase:RU000611};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001480-2,
CC ECO:0000256|RuleBase:RU000611};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR001480-2,
CC ECO:0000256|RuleBase:RU000611};
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. {ECO:0000256|ARBA:ARBA00004666,
CC ECO:0000256|RuleBase:RU004248}.
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC {ECO:0000256|ARBA:ARBA00010772, ECO:0000256|RuleBase:RU004189}.
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DR EMBL; CH408156; EDK38036.2; -; Genomic_DNA.
DR RefSeq; XP_001486463.1; XM_001486413.1.
DR AlphaFoldDB; A5DFT3; -.
DR STRING; 294746.A5DFT3; -.
DR GeneID; 5128444; -.
DR KEGG; pgu:PGUG_02134; -.
DR VEuPathDB; FungiDB:PGUG_02134; -.
DR eggNOG; KOG2757; Eukaryota.
DR HOGENOM; CLU_026967_0_0_1; -.
DR InParanoid; A5DFT3; -.
DR OMA; DIGLFCG; -.
DR OrthoDB; 1116301at2759; -.
DR UniPathway; UPA00126; UER00423.
DR Proteomes; UP000001997; Unassembled WGS sequence.
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 CDD; cd07011; cupin_PMI_type_I_N; 1.
DR Gene3D; 2.60.120.10; Jelly Rolls; 2.
DR Gene3D; 1.10.441.10; Phosphomannose Isomerase, domain 2; 1.
DR InterPro; IPR001250; Man6P_Isoase-1.
DR InterPro; IPR016305; Mannose-6-P_Isomerase.
DR InterPro; IPR018050; Pmannose_isomerase-type1_CS.
DR InterPro; IPR046456; PMI_typeI_C.
DR InterPro; IPR046457; PMI_typeI_cat.
DR InterPro; IPR046458; PMI_typeI_hel.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR NCBIfam; TIGR00218; manA; 1.
DR PANTHER; PTHR10309; MANNOSE-6-PHOSPHATE ISOMERASE; 1.
DR PANTHER; PTHR10309:SF0; MANNOSE-6-PHOSPHATE ISOMERASE; 1.
DR Pfam; PF01238; PMI_typeI_C; 1.
DR Pfam; PF20511; PMI_typeI_cat; 1.
DR Pfam; PF20512; PMI_typeI_hel; 1.
DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1.
DR PRINTS; PR00714; MAN6PISMRASE.
DR SUPFAM; SSF51182; RmlC-like cupins; 1.
DR PROSITE; PS00965; PMI_I_1; 1.
DR PROSITE; PS00966; PMI_I_2; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU000611};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001480-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001997};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001480-2}.
FT DOMAIN 3..152
FT /note="Phosphomannose isomerase type I catalytic"
FT /evidence="ECO:0000259|Pfam:PF20511"
FT DOMAIN 169..263
FT /note="Phosphomannose isomerase type I helical insertion"
FT /evidence="ECO:0000259|Pfam:PF20512"
FT DOMAIN 344..390
FT /note="Phosphomannose isomerase type I C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01238"
FT ACT_SITE 301
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-1"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
SQ SEQUENCE 429 AA; 47142 MW; 3890177374C743B0 CRC64;
MSVFRINCGY QNYDWGKVGS SSAVAQFAST SDPSITIDEK KPYAELWMGT HPSVPSTVVS
GGKSGQTLRD LVTEDPSKHL HASIVKKFGA QLPFLFKVLS IEKVLSIQAH PDKQLAKQLH
TNDPKNYPDD NHKPEMAIAV TSFEGFCGFK PLSELAKTLK TVPELTSVIG DLLVEEFCNG
ITPDATAGSQ EDVENRKLLQ KVFGKLMNTD DATINARAAE LVERTKSQPE VFTAISPKLP
ELIQRLNKQF PNDIGLFCGC LLLNHVILAP GEAMFLQAKD PHAYINGDII ECMAASDNVV
RAGFTPKFKD VKNLVDMLTY SYDSVEKQKM PLLPFAKSSG DAKSVLYDPP IEEFAVLQTL
FTEANQLQHF DKFNGPSILI ATKGSGSIVV QGSKQEVKKG YVYFIGPGAE VDLHSSEPEF
TTYRAFVEV
//
