MANB_METJA
ID MANB_METJA Reviewed; 449 AA.
AC Q57842;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Phosphomannomutase {ECO:0000303|PubMed:17014089};
DE Short=PMM;
DE EC=5.4.2.8 {ECO:0000269|PubMed:17014089};
DE AltName: Full=Phosphoglucomutase {ECO:0000303|PubMed:17014089};
GN Name=manB; OrderedLocusNames=MJ0399;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS A PHOSPHOMANNOMUTASE, SUBSTRATE SPECIFICITY, CATALYTIC
RP ACTIVITY, AND PATHWAY.
RX PubMed=17014089; DOI=10.1021/bi061018a;
RA White R.H., Xu H.;
RT "Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-
RT ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis
RT in Methanocaldococcus jannaschii.";
RL Biochemistry 45:12366-12379(2006).
CC -!- FUNCTION: Catalyzes the formation of mannose-1-P from mannose-6-P. Can
CC also use glucose-6-P. {ECO:0000269|PubMed:17014089}.
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:17014089};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11142;
CC Evidence={ECO:0000269|PubMed:17014089};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P26276};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P26276};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000305|PubMed:17014089}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; L77117; AAB98388.1; -; Genomic_DNA.
DR PIR; G64349; G64349.
DR AlphaFoldDB; Q57842; -.
DR SMR; Q57842; -.
DR STRING; 243232.MJ_0399; -.
DR EnsemblBacteria; AAB98388; AAB98388; MJ_0399.
DR KEGG; mja:MJ_0399; -.
DR eggNOG; arCOG00767; Archaea.
DR HOGENOM; CLU_016950_9_2_2; -.
DR InParanoid; Q57842; -.
DR OMA; HSGEINF; -.
DR PhylomeDB; Q57842; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004615; F:phosphomannomutase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR016066; A-D-PHexomutase_CS.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
DR PROSITE; PS00710; PGM_PMM; 1.
PE 1: Evidence at protein level;
KW Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..449
FT /note="Phosphomannomutase"
FT /id="PRO_0000147831"
FT ACT_SITE 97
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P26276"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P26276"
SQ SEQUENCE 449 AA; 51474 MW; 1EB07EEAB409BA00 CRC64;
MFGDLMVFKA YDIRGIYGRE LDENFAYSLG KCIGKKFENK KILVGNDVRI GSKELLPYFI
VGLKEYADVF YAGTISTPLM YFGTKGKYDL GVILTASHNP PEYTGFKMCD KEAIPLSPIE
EIKPIFKKYE LTESIKEEAK NLNLDDLKVN IIEEYKKFFL KRCKASDKKI AVDFANGATT
IAEKEILNEL FDNAVFINDY PDGNFPAHQP DTLKMECLKD IIRAVKKNNC ELGLIFDGDG
DRLGIVDENG NVLRGDILTA IIAKEILKEK SNAKIVYDLR CSKIVPEIIE KYGGIAIKSR
VGHYFIKKLM HEIDAEFAGE LSNHFYFKEI GYFESPLLAL NYILKAMDEE NKSLSELNKE
FSKYPHSGEI NFRVKDQKYI MEKIKEHFKD CKLEELDGIS IYCKNFWFNL RPSNTEPLLR
LNLEADDEKT MKEKVEEIKN LIAKLDASL