ID   PMM1_HUMAN              Reviewed;         262 AA.
AC   Q92871; A8K003; Q92586;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=Phosphomannomutase 1 {ECO:0000303|PubMed:9070917};
DE            Short=PMM 1 {ECO:0000303|PubMed:9070917};
DE            EC=5.4.2.8 {ECO:0000303|PubMed:16540464};
DE   AltName: Full=PMMH-22;
GN   Name=PMM1; Synonyms=PMMH22;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=9070917; DOI=10.1006/geno.1996.4536;
RA   Matthijs G., Schollen E., Pirard M., Budarf M.L., van Schaftingen E.,
RA   Cassiman J.-J.;
RT   "PMM (PMM1), the human homologue of SEC53 or yeast phosphomannomutase, is
RT   localized on chromosome 22q13.";
RL   Genomics 40:41-47(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9119384; DOI=10.1006/geno.1996.4487;
RA   Wada Y., Sakamoto M.;
RT   "Isolation of the human phosphomannomutase gene (PMM1) and assignment to
RT   chromosome 22q13.";
RL   Genomics 39:416-417(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Hansen S.H., Frank S.R., Casanova J.E.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP   MANNOSE 1-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR,
RP   SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16540464; DOI=10.1074/jbc.m601505200;
RA   Silvaggi N.R., Zhang C., Lu Z., Dai J., Dunaway-Mariano D., Allen K.N.;
RT   "The X-ray crystal structures of human alpha-phosphomannomutase 1 reveal
RT   the structural basis of congenital disorder of glycosylation type 1a.";
RL   J. Biol. Chem. 281:14918-14926(2006).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND
RP   INOSINE MONOPHOSPHATE.
RX   PubMed=29695157; DOI=10.1021/acs.biochem.8b00223;
RA   Ji T., Zhang C., Zheng L., Dunaway-Mariano D., Allen K.N.;
RT   "Structural basis of the molecular switch between phosphatase and mutase
RT   functions of human phosphomannomutase 1 under ischemic conditions.";
RL   Biochemistry 57:3480-3492(2018).
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. In addition, may be responsible for the degradation of
CC       glucose-1,6-bisphosphate in ischemic brain.
CC       {ECO:0000269|PubMed:16540464}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate;
CC         Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735;
CC         EC=5.4.2.8; Evidence={ECO:0000269|PubMed:16540464};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:16540464};
CC   -!- ACTIVITY REGULATION: IMP, a metabolite whose concentration is elevated
CC       in anoxia, inhibits phosphomannomutase and phosphoglucomutase
CC       activities and strongly enhances glucose-1,6-bisphosphatase activity.
CC       {ECO:0000250|UniProtKB:O35621}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=54 uM for alpha-D-mannose 1-phosphate
CC         {ECO:0000269|PubMed:16540464};
CC         KM=7.5 uM for alpha-D-glucose 1-phosphate
CC         {ECO:0000269|PubMed:16540464};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate:
CC       step 2/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16540464}.
CC   -!- INTERACTION:
CC       Q92871; P20340: RAB6A; NbExp=4; IntAct=EBI-746784, EBI-1052826;
CC       Q92871; P20340-2: RAB6A; NbExp=3; IntAct=EBI-746784, EBI-8840191;
CC       Q92871; Q9NRW1: RAB6B; NbExp=5; IntAct=EBI-746784, EBI-1760079;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35621}.
CC   -!- TISSUE SPECIFICITY: Strong expression in liver, heart, brain, and
CC       pancreas; lower expression in skeletal muscle.
CC   -!- SIMILARITY: Belongs to the eukaryotic PMM family. {ECO:0000305}.
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DR   EMBL; U62526; AAC51117.1; -; mRNA.
DR   EMBL; D87810; BAA13460.1; -; mRNA.
DR   EMBL; U86070; AAC00023.1; -; mRNA.
DR   EMBL; CR456544; CAG30430.1; -; mRNA.
DR   EMBL; AK289368; BAF82057.1; -; mRNA.
DR   EMBL; AK316580; BAG38168.1; -; mRNA.
DR   EMBL; AL023553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471095; EAW60443.1; -; Genomic_DNA.
DR   EMBL; BC010855; AAH10855.1; -; mRNA.
DR   EMBL; BC016818; AAH16818.1; -; mRNA.
DR   CCDS; CCDS14020.1; -.
DR   RefSeq; NP_002667.2; NM_002676.2.
DR   PDB; 2FUC; X-ray; 2.10 A; A=1-262.
DR   PDB; 2FUE; X-ray; 1.75 A; A=1-262.
DR   PDB; 6CFR; X-ray; 2.07 A; A=1-262.
DR   PDB; 6CFS; X-ray; 2.07 A; A=1-262.
DR   PDB; 6CFT; X-ray; 2.43 A; A=1-262.
DR   PDB; 6CFU; X-ray; 2.24 A; A=1-262.
DR   PDB; 6CFV; X-ray; 1.92 A; A=1-262.
DR   PDBsum; 2FUC; -.
DR   PDBsum; 2FUE; -.
DR   PDBsum; 6CFR; -.
DR   PDBsum; 6CFS; -.
DR   PDBsum; 6CFT; -.
DR   PDBsum; 6CFU; -.
DR   PDBsum; 6CFV; -.
DR   AlphaFoldDB; Q92871; -.
DR   SMR; Q92871; -.
DR   BioGRID; 111385; 20.
DR   ComplexPortal; CPX-2131; alpha-D-mannose 1,6-phosphomutase.
DR   IntAct; Q92871; 14.
DR   MINT; Q92871; -.
DR   STRING; 9606.ENSP00000216259; -.
DR   iPTMnet; Q92871; -.
DR   PhosphoSitePlus; Q92871; -.
DR   BioMuta; PMM1; -.
DR   DMDM; 2499519; -.
DR   EPD; Q92871; -.
DR   jPOST; Q92871; -.
DR   MassIVE; Q92871; -.
DR   MaxQB; Q92871; -.
DR   PaxDb; 9606-ENSP00000216259; -.
DR   PeptideAtlas; Q92871; -.
DR   ProteomicsDB; 75557; -.
DR   Pumba; Q92871; -.
DR   Antibodypedia; 26980; 115 antibodies from 21 providers.
DR   DNASU; 5372; -.
DR   Ensembl; ENST00000216259.8; ENSP00000216259.7; ENSG00000100417.12.
DR   GeneID; 5372; -.
DR   KEGG; hsa:5372; -.
DR   MANE-Select; ENST00000216259.8; ENSP00000216259.7; NM_002676.3; NP_002667.2.
DR   UCSC; uc003bal.3; human.
DR   AGR; HGNC:9114; -.
DR   CTD; 5372; -.
DR   DisGeNET; 5372; -.
DR   GeneCards; PMM1; -.
DR   HGNC; HGNC:9114; PMM1.
DR   HPA; ENSG00000100417; Low tissue specificity.
DR   MIM; 601786; gene.
DR   neXtProt; NX_Q92871; -.
DR   OpenTargets; ENSG00000100417; -.
DR   PharmGKB; PA33440; -.
DR   VEuPathDB; HostDB:ENSG00000100417; -.
DR   eggNOG; KOG3189; Eukaryota.
DR   GeneTree; ENSGT00390000002918; -.
DR   HOGENOM; CLU_065642_0_1_1; -.
DR   InParanoid; Q92871; -.
DR   OMA; FCLHYMA; -.
DR   OrthoDB; 167037at2759; -.
DR   PhylomeDB; Q92871; -.
DR   TreeFam; TF300874; -.
DR   BRENDA; 5.4.2.8; 2681.
DR   PathwayCommons; Q92871; -.
DR   Reactome; R-HSA-446205; Synthesis of GDP-mannose.
DR   SABIO-RK; Q92871; -.
DR   SignaLink; Q92871; -.
DR   UniPathway; UPA00126; UER00424.
DR   BioGRID-ORCS; 5372; 10 hits in 1170 CRISPR screens.
DR   ChiTaRS; PMM1; human.
DR   EvolutionaryTrace; Q92871; -.
DR   GeneWiki; PMM1; -.
DR   GenomeRNAi; 5372; -.
DR   Pharos; Q92871; Tbio.
DR   PRO; PR:Q92871; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q92871; Protein.
DR   Bgee; ENSG00000100417; Expressed in lower esophagus mucosa and 187 other cell types or tissues.
DR   ExpressionAtlas; Q92871; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004615; F:phosphomannomutase activity; IDA:UniProtKB.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; TAS:Reactome.
DR   GO; GO:0006013; P:mannose metabolic process; IDA:UniProtKB.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR   CDD; cd02585; HAD_PMM; 1.
DR   Gene3D; 3.30.1240.20; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR005002; PMM.
DR   InterPro; IPR043169; PMM_cap.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   PANTHER; PTHR10466; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR10466:SF1; PHOSPHOMANNOMUTASE 1; 1.
DR   Pfam; PF03332; PMM; 1.
DR   SFLD; SFLDF00445; alpha-phosphomannomutase; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   Genevisible; Q92871; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Isomerase; Magnesium; Metal-binding;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..262
FT                   /note="Phosphomannomutase 1"
FT                   /id="PRO_0000199692"
FT   ACT_SITE        19
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:16540464"
FT   ACT_SITE        21
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000269|PubMed:16540464"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16540464,
FT                   ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT   BINDING         21
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16540464,
FT                   ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT   BINDING         28
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000269|PubMed:16540464"
FT   BINDING         132
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000269|PubMed:16540464"
FT   BINDING         143
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000269|PubMed:16540464"
FT   BINDING         150
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000269|PubMed:16540464"
FT   BINDING         186
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000269|PubMed:16540464"
FT   BINDING         188
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000269|PubMed:16540464"
FT   BINDING         190
FT                   /ligand="alpha-D-mannose 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58409"
FT                   /evidence="ECO:0000269|PubMed:16540464"
FT   BINDING         218
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:16540464,
FT                   ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:16540464,
FT                   ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:16540464,
FT                   ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT   BINDING         235
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:16540464,
FT                   ECO:0007744|PDB:2FUC, ECO:0007744|PDB:2FUE"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         242
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35621"
FT   CONFLICT        11
FT                   /note="K -> R (in Ref. 1; AAC51117)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        169
FT                   /note="A -> D (in Ref. 1; AAC51117)"
FT                   /evidence="ECO:0000305"
FT   STRAND          14..21
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   TURN            22..24
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           33..42
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   TURN            43..45
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           56..63
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           69..72
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          83..86
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:2FUC"
FT   HELIX           96..100
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           102..117
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           147..160
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           162..173
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   TURN            174..176
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          179..182
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          189..193
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           198..201
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           202..205
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   TURN            206..209
FT                   /evidence="ECO:0007829|PDB:2FUC"
FT   STRAND          211..218
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           227..231
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   STRAND          235..239
FT                   /evidence="ECO:0007829|PDB:2FUE"
FT   HELIX           243..254
FT                   /evidence="ECO:0007829|PDB:2FUE"
SQ   SEQUENCE   262 AA;  29747 MW;  1FBA7BFC9C3BB0BB CRC64;
     MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV VGGSDYCKIA
     EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR
     LPKKRGTFIE FRNGMLNISP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR
     FSRGGMISFD VFPEGWDKRY CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV
     VSPQDTVQRC REIFFPETAH EA
//