ID V4CR43_LOTGI Unreviewed; 414 AA.
AC V4CR43;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Mannose-6-phosphate isomerase {ECO:0000256|ARBA:ARBA00011956, ECO:0000256|RuleBase:RU000611};
DE EC=5.3.1.8 {ECO:0000256|ARBA:ARBA00011956, ECO:0000256|RuleBase:RU000611};
DE Flags: Fragment;
GN ORFNames=LOTGIDRAFT_109203 {ECO:0000313|EMBL:ESP04950.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP04950.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESP04950.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(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: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; KB199651; ESP04950.1; -; Genomic_DNA.
DR RefSeq; XP_009044459.1; XM_009046211.1.
DR AlphaFoldDB; V4CR43; -.
DR STRING; 225164.V4CR43; -.
DR EnsemblMetazoa; LotgiT109203; LotgiP109203; LotgiG109203.
DR GeneID; 20230439; -.
DR KEGG; lgi:LOTGIDRAFT_109203; -.
DR CTD; 20230439; -.
DR HOGENOM; CLU_026967_0_0_1; -.
DR OMA; DIGLFCG; -.
DR OrthoDB; 1116301at2759; -.
DR UniPathway; UPA00126; UER00423.
DR Proteomes; UP000030746; 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:UP000030746};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001480-2}.
FT DOMAIN 2..144
FT /note="Phosphomannose isomerase type I catalytic"
FT /evidence="ECO:0000259|Pfam:PF20511"
FT DOMAIN 163..250
FT /note="Phosphomannose isomerase type I helical insertion"
FT /evidence="ECO:0000259|Pfam:PF20512"
FT DOMAIN 331..373
FT /note="Phosphomannose isomerase type I C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01238"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-1"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR001480-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ESP04950.1"
SQ SEQUENCE 414 AA; 45997 MW; 2F984114FA3961AA CRC64;
VFLLKCGVQE YAWGKVGSDS EVAKLAQAGN KDFQLKDNAP YAELWMGTHP NCPSFIDGTE
TTLEQWIKDN PDKLGSEVKK DFGGKLPFLF KVLSVQKSLS IQAHPHKVLA EHLHKTRPDI
YKDPNHKPEM AIALTPFQGL CGFRVLKEIA EYVQEIEELR NVIGCQTACK FITASMATDM
LLQREALKDA FKGLMEQDKE IIQTQLHKLV SRVKLLKENG EDISAYNGDL LLKLDNEFPG
DVGGFAIYFL NIITLQPGEA MFLEADMPHA YLSGDCMECM ACSDNVVRAG LTPKFIDVHT
LCEMLDYTCK PISKTRFQGI EQNNDIKVTQ FNPPVPDFSV TRFEIPDNVK TTKIAPINSA
SISIVIQGEG HITNPTLATP ISIQRGSVLF TGAMEDLELQ VKSDVLLFRA SAGL
//