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 01-MAY-2013, entry version 93.
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=10.1016/0378-1097(93)90142-O;
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; VIETQQS; -.
DR ProtClustDB; CLSK698862; -.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; IEA: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 PANTHER; PTHR18964:SF1; PTHR18964:SF1; 1.
DR Pfam; PF01238; PMI_typeI; 1.
DR PIRSF; PIRSF036894; PMI_Firm_short; 1.
DR SUPFAM; SSF51182; RmlC_like_cupin; 1.
DR TIGRFAMs; TIGR00218; manA; 1.
DR PROSITE; PS00965; PMI_I_1; FALSE_NEG.
DR PROSITE; PS00966; PMI_I_2; FALSE_NEG.
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
//
