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   27-MAR-2024, entry version 123.
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   PaxDb; 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   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   CDD; cd03089; PMM_PGM; 1.
DR   Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR   Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
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   PANTHER; PTHR43771; PHOSPHOMANNOMUTASE; 1.
DR   PANTHER; PTHR43771:SF1; PHOSPHOMANNOMUTASE; 1.
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; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR   SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
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
//