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Database: UniProt
Entry: Q59935
LinkDB: Q59935
Original site: Q59935 
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   09-JUL-2014, entry version 101.
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
RT   phosphomannose 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.,
RA   Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P.,
RA   Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A.,
RA   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: D-mannose 6-phosphate = D-fructose 6-
CC       phosphate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1
CC       family.
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DR   EMBL; D16594; BAA04021.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59462.1; -; Genomic_DNA.
DR   RefSeq; NP_722156.1; NC_004350.2.
DR   ProteinModelPortal; Q59935; -.
DR   SMR; Q59935; 2-312.
DR   STRING; 210007.SMU.1839; -.
DR   EnsemblBacteria; AAN59462; AAN59462; SMU_1839.
DR   GeneID; 1029052; -.
DR   KEGG; smu:SMU_1839; -.
DR   PATRIC; 19665675; VBIStrMut61772_1642.
DR   eggNOG; COG1482; -.
DR   KO; K01809; -.
DR   OMA; PKAKEFP; -.
DR   OrthoDB; EOG66MQQS; -.
DR   PhylomeDB; Q59935; -.
DR   BioCyc; SMUT210007:GC7Z-1741-MONOMER; -.
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.
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   Complete proteome; Isomerase; Metal-binding; Zinc.
FT   CHAIN         1    316       Mannose-6-phosphate isomerase.
FT                                /FTId=PRO_0000194229.
FT   ACT_SITE    191    191       By similarity.
FT   METAL        95     95       Zinc (By similarity).
FT   METAL        97     97       Zinc (By similarity).
FT   METAL       114    114       Zinc (By similarity).
FT   METAL       171    171       Zinc (By similarity).
FT   CONFLICT      2      3       AE -> EG (in Ref. 1; BAA04021).
FT   CONFLICT    175    175       K -> R (in Ref. 1; BAA04021).
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
//
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