ID   MANA_STRMU              Reviewed;         316 AA.
AC   Q59935;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Mannose-6-phosphate isomerase;
DE            EC=5.3.1.8;
DE   AltName: Full=Phosphohexomutase;
DE   AltName: Full=Phosphomannose isomerase;
DE            Short=PMI;
GN   Name=pmi; Synonyms=manA; OrderedLocusNames=SMU_1839;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GS-5;
RX   PubMed=8293960; DOI=10.1111/j.1574-6968.1993.tb06551.x;
RA   Sato Y., Yamamoto Y., Kizaki H., Kuramitsu H.K.;
RT   "Isolation and sequence analysis of the pmi gene encoding phosphomannose
RT   isomerase of Streptococcus mutans.";
RL   FEMS Microbiol. Lett. 114:61-66(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D16594; BAA04021.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59462.1; -; Genomic_DNA.
DR   RefSeq; NP_722156.1; NC_004350.2.
DR   RefSeq; WP_002262655.1; NC_004350.2.
DR   AlphaFoldDB; Q59935; -.
DR   SMR; Q59935; -.
DR   STRING; 210007.SMU_1839; -.
DR   PRIDE; Q59935; -.
DR   EnsemblBacteria; AAN59462; AAN59462; SMU_1839.
DR   KEGG; smu:SMU_1839; -.
DR   PATRIC; fig|210007.7.peg.1642; -.
DR   eggNOG; COG1482; Bacteria.
DR   HOGENOM; CLU_020529_0_0_9; -.
DR   OMA; FRPKIWG; -.
DR   PhylomeDB; Q59935; -.
DR   Proteomes; UP000002512; Chromosome.
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   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR001250; Man6P_Isoase-1.
DR   InterPro; IPR014628; Man6P_isomerase_Firm_short.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF01238; PMI_typeI; 1.
DR   PIRSF; PIRSF036894; PMI_Firm_short; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
DR   TIGRFAMs; TIGR00218; manA; 1.
PE   3: Inferred from homology;
KW   Isomerase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..316
FT                   /note="Mannose-6-phosphate isomerase"
FT                   /id="PRO_0000194229"
FT   ACT_SITE        191
FT                   /evidence="ECO:0000250|UniProtKB:P34948"
FT   BINDING         95
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39841"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39841"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P39841"
FT   CONFLICT        2..3
FT                   /note="AE -> EG (in Ref. 1; BAA04021)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="K -> R (in Ref. 1; BAA04021)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   316 AA;  35374 MW;  1DBF0411DA6CCF33 CRC64;
     MAEPLFLQSQ MHKKIWGGNR LRKEFGYDIP SETTGEYWAI SAHPNGVSVV KNGVYKGVPL
     DELYAEHREL FGNSKSSVFP LLTKILDAND WLSVQVHPDN AYALEHEGEL GKTECWYVIS
     ADEGAEIIYG HEAKSKEELR QMIAAGDWDH LLTKIPVKAG DFFYVPSGTM HAIGKGIMIL
     ETQQSSDTTY RVYDFDRKDD QGRKRALHIE QSIDVLTIGK PANATPAWLS LQGLETTVLV
     SSPFFTVYKW QISGSVKMQQ TAPYLLVSVL AGQGRITVGL EQYALRKGDH LILPNTIKSW
     QFDGDLEIIA SHSNEC