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Database: UniProt/TrEMBL
Entry: V4CR43_LOTGI
LinkDB: V4CR43_LOTGI
Original site: V4CR43_LOTGI 
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
//
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