PMGE_HUMAN
ID PMGE_HUMAN Reviewed; 259 AA.
AC P07738; A4D1N9;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Bisphosphoglycerate mutase;
DE Short=BPGM;
DE EC=5.4.2.4 {ECO:0000269|PubMed:21045285};
DE AltName: Full=2,3-bisphosphoglycerate mutase, erythrocyte;
DE AltName: Full=2,3-bisphosphoglycerate synthase;
DE EC=5.4.2.11 {ECO:0000269|PubMed:21045285};
DE AltName: Full=2,3-diphosphoglycerate mutase;
DE Short=DPGM;
DE AltName: Full=BPG-dependent PGAM;
GN Name=BPGM;
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 PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY,
RP IDENTIFICATION OF VARIANT ECYT8 CYS-90, CHARACTERIZATION OF VARIANT ECYT8
RP CYS-90, AND INVOLVEMENT IN ECYT8.
RX PubMed=2542247; DOI=10.1016/s0021-9258(18)83118-0;
RA Rosa R., Blouquit Y., Calvin M.C., Prome D., Prome J.C., Rosa J.;
RT "Isolation, characterization, and structure of a mutant 89 ArgTO:
RT bisphosphoglycerate mutase. Implication of the active site in the
RT mutation.";
RL J. Biol. Chem. 264:7837-7843(1989).
RN [2]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-259, CLEAVAGE OF INITIATOR METHIONINE,
RP AND TISSUE SPECIFICITY.
RX PubMed=6313356; DOI=10.1002/j.1460-2075.1983.tb01569.x;
RA Haggarty N.W., Dunbar B., Fothergill L.A.;
RT "The complete amino acid sequence of human erythrocyte diphosphoglycerate
RT mutase.";
RL EMBO J. 2:1213-1220(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=3023066; DOI=10.1002/j.1460-2075.1986.tb04495.x;
RA Joulin V., Peduzzi J., Romeo P.-H., Rosa R., Valentin C., Dubart A.,
RA Lapeyre B., Blouquit Y., Garel M.-C., Goossens M., Rosa J., Cohen-Solal M.;
RT "Molecular cloning and sequencing of the human erythrocyte 2,3-
RT bisphosphoglycerate mutase cDNA: revised amino acid sequence.";
RL EMBO J. 5:2275-2283(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3036106;
RA Cohen-Solal M., Joulin V., Romeo P.-H., Rosa R., Valentin C., Garel M.-C.,
RA Rosa J.;
RT "Molecular cloning of the human 2,3-bisphosphoglycerate mutase cDNA and
RT revised amino acid sequence.";
RL Biomed. Biochim. Acta 46:S126-S130(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2844822; DOI=10.1016/s0021-9258(19)37657-4;
RA Joulin V., Garel M.-C., le Boulch P., Valentin C., Rosa R., Rosa J.,
RA Cohen-Solal M.;
RT "Isolation and characterization of the human 2,3-bisphosphoglycerate mutase
RT gene.";
RL J. Biol. Chem. 263:15785-15790(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [10]
RP PROTEIN SEQUENCE OF 2-46; 144-168 AND 182-206, GLYCATION AT LYS-3; LYS-5;
RP LYS-18; LYS-43; LYS-159 AND LYS-197, AND LACK OF GLYCATION AT LYS-29;
RP LYS-46; LYS-143; LYS-181; LYS-246; LYS-247; LYS-253; LYS-258 AND LYS-259.
RX PubMed=9832630; DOI=10.1093/oxfordjournals.jbchem.a022243;
RA Fujita T., Suzuki K., Tada T., Yoshihara Y., Hamaoka R., Uchida K.,
RA Matuo Y., Sasaki T., Hanafusa T., Taniguchi N.;
RT "Human erythrocyte bisphosphoglycerate mutase: inactivation by glycation in
RT vivo and in vitro.";
RL J. Biochem. 124:1237-1244(1998).
RN [11]
RP PROTEIN SEQUENCE OF 104-114.
RX PubMed=8440681; DOI=10.1016/s0021-9258(18)53552-3;
RA Stafforini D.M., Rollins E.N., Prescott S.M., McIntyre T.M.;
RT "The platelet-activating factor acetylhydrolase from human erythrocytes.
RT Purification and properties.";
RL J. Biol. Chem. 268:3857-3865(1993).
RN [12]
RP ACTIVITY REGULATION.
RX PubMed=10477269; DOI=10.1042/bj3420581;
RA Mulquiney P.J., Kuchel P.W.;
RT "Model of 2,3-bisphosphoglycerate metabolism in the human erythrocyte based
RT on detailed enzyme kinetic equations: equations and parameter refinement.";
RL Biochem. J. 342:581-596(1999).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=16246416; DOI=10.1016/j.placenta.2005.08.010;
RA Pritlove D.C., Gu M., Boyd C.A., Randeva H.S., Vatish M.;
RT "Novel placental expression of 2,3-bisphosphoglycerate mutase.";
RL Placenta 27:924-927(2006).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP 3D-STRUCTURE MODELING.
RX PubMed=1387804; DOI=10.1016/0300-9084(92)90149-9;
RA Craescu C.T., Schaad O., Garel M.-C., Rosa R., Edelstein S.J.;
RT "Structural modeling of the human erythrocyte bisphosphoglycerate mutase.";
RL Biochimie 74:519-526(1992).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-259, AND SUBUNIT.
RX PubMed=15258155; DOI=10.1074/jbc.m405982200;
RA Wang Y., Wei Z., Bian Q., Cheng Z., Wan M., Liu L., Gong W.;
RT "Crystal structure of human bisphosphoglycerate mutase.";
RL J. Biol. Chem. 279:39132-39138(2004).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-258 IN COMPLEXES WITH
RP 3-PHOSPHO-D-GLYCERATE AND 2,3-BISPHOSPHO-D-GLYCERATE, SUBUNIT, AND ACTIVE
RP SITE.
RX PubMed=17052986; DOI=10.1074/jbc.m606421200;
RA Wang Y., Liu L., Wei Z., Cheng Z., Lin Y., Gong W.;
RT "Seeing the process of histidine phosphorylation in human
RT bisphosphoglycerate mutase.";
RL J. Biol. Chem. 281:39642-39648(2006).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP ACTIVITY REGULATION.
RX PubMed=21045285; DOI=10.1107/s1744309110035475;
RA Patterson A., Price N.C., Nairn J.;
RT "Unliganded structure of human bisphosphoglycerate mutase reveals side-
RT chain movements induced by ligand binding.";
RL Acta Crystallogr. F 66:1415-1420(2010).
RN [21]
RP VARIANT ECYT8 CYS-90.
RX PubMed=1421379;
RA Lemarchandel V., Joulin V., Valentin C., Rosa R., Galacteros F., Rosa J.,
RA Cohen-Solal M.;
RT "Compound heterozygosity in a complete erythrocyte bisphosphoglycerate
RT mutase deficiency.";
RL Blood 80:2643-2649(1992).
RN [22]
RP VARIANT ECYT8 GLN-62.
RX PubMed=15054810; DOI=10.1002/ajh.20014;
RA Hoyer J.D., Allen S.L., Beutler E., Kubik K., West C., Fairbanks V.F.;
RT "Erythrocytosis due to bisphosphoglycerate mutase deficiency with
RT concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency.";
RL Am. J. Hematol. 75:205-208(2004).
CC -!- FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity
CC by controlling the levels of its allosteric effector 2,3-
CC bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11)
CC activity. {ECO:0000269|PubMed:21045285}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-
CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4;
CC Evidence={ECO:0000269|PubMed:21045285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000269|PubMed:21045285};
CC -!- ACTIVITY REGULATION: At alkaline pH BPGM favors the synthase reaction;
CC however, at lower pH the phosphatase reaction is dominant. Inhibited by
CC citrate. {ECO:0000269|PubMed:10477269, ECO:0000269|PubMed:21045285}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15258155,
CC ECO:0000269|PubMed:17052986}.
CC -!- INTERACTION:
CC P07738; P15259: PGAM2; NbExp=4; IntAct=EBI-2115835, EBI-2511669;
CC -!- TISSUE SPECIFICITY: Expressed in red blood cells. Expressed in non-
CC erythroid cells of the placenta; present in the syncytiotrophoblast
CC layer of the placental villi at the feto-maternal interface (at protein
CC level). {ECO:0000269|PubMed:16246416, ECO:0000269|PubMed:3023066,
CC ECO:0000269|PubMed:6313356}.
CC -!- PTM: Glycation of Lys-159 in diabetic patients inactivates the enzyme.
CC -!- DISEASE: Erythrocytosis, familial, 8 (ECYT8) [MIM:222800]: An autosomal
CC recessive disorder characterized by elevated serum hemoglobin and
CC hematocrit, and biphosphoglycerate mutase deficiency. ECYT8 affected
CC individuals manifest hemolytic anemia and splenomegaly.
CC {ECO:0000269|PubMed:1421379, ECO:0000269|PubMed:15054810,
CC ECO:0000269|PubMed:2542247}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; X04327; CAA27858.1; -; mRNA.
DR EMBL; M23068; AAA51840.1; -; Genomic_DNA.
DR EMBL; M23067; AAA51840.1; JOINED; Genomic_DNA.
DR EMBL; AK315439; BAG37827.1; -; mRNA.
DR EMBL; CH236950; EAL24067.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83821.1; -; Genomic_DNA.
DR EMBL; BC017050; AAH17050.1; -; mRNA.
DR CCDS; CCDS5833.1; -.
DR PIR; A31999; PMHUBM.
DR RefSeq; NP_001280014.1; NM_001293085.1.
DR RefSeq; NP_001715.1; NM_001724.4.
DR RefSeq; NP_954655.1; NM_199186.2.
DR RefSeq; XP_011514829.1; XM_011516527.1.
DR PDB; 1T8P; X-ray; 2.50 A; A/B=1-259.
DR PDB; 2A9J; X-ray; 2.00 A; A/B=1-259.
DR PDB; 2F90; X-ray; 2.00 A; A/B=1-259.
DR PDB; 2H4X; X-ray; 1.85 A; A/B=1-259.
DR PDB; 2H4Z; X-ray; 2.00 A; A/B=1-259.
DR PDB; 2H52; X-ray; 2.00 A; A/B=1-259.
DR PDB; 2HHJ; X-ray; 1.50 A; A/B=1-259.
DR PDB; 3NFY; X-ray; 1.94 A; A/B=1-259.
DR PDB; 7N3R; X-ray; 2.25 A; A/B=1-259.
DR PDB; 7N3S; X-ray; 2.48 A; A/B=1-259.
DR PDB; 7THI; X-ray; 1.33 A; A/B=1-259.
DR PDBsum; 1T8P; -.
DR PDBsum; 2A9J; -.
DR PDBsum; 2F90; -.
DR PDBsum; 2H4X; -.
DR PDBsum; 2H4Z; -.
DR PDBsum; 2H52; -.
DR PDBsum; 2HHJ; -.
DR PDBsum; 3NFY; -.
DR PDBsum; 7N3R; -.
DR PDBsum; 7N3S; -.
DR PDBsum; 7THI; -.
DR AlphaFoldDB; P07738; -.
DR SMR; P07738; -.
DR BioGRID; 107137; 27.
DR IntAct; P07738; 18.
DR STRING; 9606.ENSP00000376840; -.
DR DEPOD; BPGM; -.
DR iPTMnet; P07738; -.
DR MetOSite; P07738; -.
DR PhosphoSitePlus; P07738; -.
DR BioMuta; BPGM; -.
DR DMDM; 130350; -.
DR REPRODUCTION-2DPAGE; IPI00215979; -.
DR EPD; P07738; -.
DR jPOST; P07738; -.
DR MassIVE; P07738; -.
DR MaxQB; P07738; -.
DR PaxDb; P07738; -.
DR PeptideAtlas; P07738; -.
DR PRIDE; P07738; -.
DR ProteomicsDB; 52025; -.
DR Antibodypedia; 2975; 265 antibodies from 28 providers.
DR DNASU; 669; -.
DR Ensembl; ENST00000344924.8; ENSP00000342032.3; ENSG00000172331.12.
DR Ensembl; ENST00000393132.2; ENSP00000376840.2; ENSG00000172331.12.
DR Ensembl; ENST00000418040.5; ENSP00000399838.1; ENSG00000172331.12.
DR GeneID; 669; -.
DR KEGG; hsa:669; -.
DR MANE-Select; ENST00000344924.8; ENSP00000342032.3; NM_001724.5; NP_001715.1.
DR UCSC; uc003vrv.4; human.
DR CTD; 669; -.
DR DisGeNET; 669; -.
DR GeneCards; BPGM; -.
DR HGNC; HGNC:1093; BPGM.
DR HPA; ENSG00000172331; Tissue enhanced (bone).
DR MalaCards; BPGM; -.
DR MIM; 222800; phenotype.
DR MIM; 613896; gene.
DR neXtProt; NX_P07738; -.
DR OpenTargets; ENSG00000172331; -.
DR Orphanet; 247378; Autosomal recessive secondary polycythemia not associated with VHL gene.
DR Orphanet; 714; Hemolytic anemia due to diphosphoglycerate mutase deficiency.
DR PharmGKB; PA25401; -.
DR VEuPathDB; HostDB:ENSG00000172331; -.
DR eggNOG; KOG0235; Eukaryota.
DR GeneTree; ENSGT00950000182926; -.
DR HOGENOM; CLU_033323_1_1_1; -.
DR InParanoid; P07738; -.
DR OMA; ITESHPY; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; P07738; -.
DR TreeFam; TF300007; -.
DR BioCyc; MetaCyc:HS10491-MON; -.
DR BRENDA; 5.4.2.4; 2681.
DR PathwayCommons; P07738; -.
DR Reactome; R-HSA-70171; Glycolysis.
DR SABIO-RK; P07738; -.
DR SignaLink; P07738; -.
DR BioGRID-ORCS; 669; 17 hits in 1084 CRISPR screens.
DR ChiTaRS; BPGM; human.
DR EvolutionaryTrace; P07738; -.
DR GenomeRNAi; 669; -.
DR Pharos; P07738; Tbio.
DR PRO; PR:P07738; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P07738; protein.
DR Bgee; ENSG00000172331; Expressed in secondary oocyte and 195 other tissues.
DR ExpressionAtlas; P07738; baseline and differential.
DR Genevisible; P07738; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; TAS:Reactome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:InterPro.
DR GO; GO:1901136; P:carbohydrate derivative catabolic process; TAS:Reactome.
DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
DR GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0060856; P:establishment of blood-brain barrier; IEA:Ensembl.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR GO; GO:0150076; P:neuroinflammatory response; IEA:Ensembl.
DR GO; GO:0015671; P:oxygen transport; IEA:Ensembl.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; TAS:ProtInc.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Congenital erythrocytosis;
KW Direct protein sequencing; Disease variant; Glycation; Glycolysis;
KW Glycoprotein; Hereditary hemolytic anemia; Hydrolase; Isomerase;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6313356,
FT ECO:0000269|PubMed:9832630, ECO:0007744|PubMed:22814378"
FT CHAIN 2..259
FT /note="Bisphosphoglycerate mutase"
FT /id="PRO_0000179834"
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:17052986"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:17052986"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17052986"
FT BINDING 23..24
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17052986"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17052986"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17052986"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17052986"
FT BINDING 116..117
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17052986"
FT BINDING 189..190
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17052986"
FT SITE 29
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9832630"
FT SITE 46
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9832630"
FT SITE 143
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9832630"
FT SITE 181
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9832630"
FT SITE 188
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000269|PubMed:17052986"
FT SITE 246
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9832630"
FT SITE 247
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9832630"
FT SITE 253
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9832630"
FT SITE 258
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9832630"
FT SITE 259
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:9832630"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 122
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 3
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:9832630"
FT CARBOHYD 5
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:9832630"
FT CARBOHYD 18
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:9832630"
FT CARBOHYD 43
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:9832630"
FT CARBOHYD 159
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:9832630"
FT CARBOHYD 197
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:9832630"
FT VARIANT 62
FT /note="R -> Q (in ECYT8; dbSNP:rs751972865)"
FT /evidence="ECO:0000269|PubMed:15054810"
FT /id="VAR_065367"
FT VARIANT 90
FT /note="R -> C (in ECYT8; mutation identified at protein
FT level; marked decrease in synthase and mutase activities;
FT no effect on phosphatase activity; dbSNP:rs121964925)"
FT /evidence="ECO:0000269|PubMed:1421379,
FT ECO:0000269|PubMed:2542247"
FT /id="VAR_065368"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 15..19
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 32..47
FT /evidence="ECO:0007829|PDB:7THI"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:7THI"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 133..137
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:7THI"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:7THI"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:7THI"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:7THI"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:7THI"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:7THI"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:7THI"
SQ SEQUENCE 259 AA; 30005 MW; A2AF1D6F2985A3B5 CRC64;
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL
NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EQMALNHGEE QVRLWRRSYN
VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG
KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA
IQAAIKKVED QGKVKQAKK
