ID G8BZV3_TETPH Unreviewed; 429 AA.
AC G8BZV3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
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 Name=TPHA0L00750 {ECO:0000313|EMBL:CCE65431.1};
GN OrderedLocusNames=TPHA_0L00750 {ECO:0000313|EMBL:CCE65431.1};
OS Tetrapisispora phaffii (strain ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL
OS Y-8282 / UCD 70-5) (Yeast) (Fabospora phaffii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071381 {ECO:0000313|EMBL:CCE65431.1, ECO:0000313|Proteomes:UP000005666};
RN [1] {ECO:0000313|EMBL:CCE65431.1, ECO:0000313|Proteomes:UP000005666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24235 / CBS 4417 / NBRC 1672 / NRRL Y-8282 / UCD 70-5
RC {ECO:0000313|Proteomes:UP000005666};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE612867; CCE65431.1; -; Genomic_DNA.
DR RefSeq; XP_003687865.1; XM_003687817.1.
DR AlphaFoldDB; G8BZV3; -.
DR STRING; 1071381.G8BZV3; -.
DR GeneID; 11531612; -.
DR KEGG; tpf:TPHA_0L00750; -.
DR eggNOG; KOG2757; Eukaryota.
DR HOGENOM; CLU_026967_0_0_1; -.
DR OMA; DIGLFCG; -.
DR OrthoDB; 1116301at2759; -.
DR UniPathway; UPA00126; UER00423.
DR Proteomes; UP000005666; Chromosome 12.
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:UP000005666};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001480-2}.
FT DOMAIN 5..153
FT /note="Phosphomannose isomerase type I catalytic"
FT /evidence="ECO:0000259|Pfam:PF20511"
FT DOMAIN 169..262
FT /note="Phosphomannose isomerase type I helical insertion"
FT /evidence="ECO:0000259|Pfam:PF20512"
FT DOMAIN 343..390
FT /note="Phosphomannose isomerase type I C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01238"
FT ACT_SITE 300
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-1"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
SQ SEQUENCE 429 AA; 47816 MW; CB66309FE3BB8772 CRC64;
MSDKVFRLNV GYQQYAWGKI GSNSSVARFA AHSDPSLKIN ENEPYAELWM GTHPKVPSYK
YGTKETLNQI ISNDPVKMLG KDIINQYQSK DEIPFLFKVL SIEKVLSIQA HPDKKLAKIL
RAQDPENYPD DNHKPEMAIA VTDFEGFCGF KPLREIATTL ENVPEFRTLV GEECSKEFIQ
FAKANVTLGS EDDKLNRKLL QKVFSKVMNA SDETIMSAAK PLVERAEKSP KDFPFEDLPE
LILRLHAQFP NDVGLFCGCL MLNHCHLKSG EAIFLKAKDP HAYINGDIIE CMAASDNVVR
AGFTPKFKDV KNLVEMLTYD ADSVDDQKMK PVAYTKSSGD GVSLLYNPPI DEFSIVSTTF
EDKVGTRKFS GVDGPSIIIT TKGNGYIIGD GAKIKAEPGF VFFVAPNIEV ELQAEDTSFV
TYRAIAEPK
//
