ID MPI_DICDI Reviewed; 452 AA.
AC Q54PA0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=Probable mannose-6-phosphate isomerase;
DE EC=5.3.1.8;
DE AltName: Full=Phosphohexomutase;
DE AltName: Full=Phosphomannose isomerase;
DE Short=PMI;
GN Name=mpi; ORFNames=DDB_G0284685;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
RA Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
RA Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Involved in the synthesis of the GDP-mannose and
CC dolichol-phosphate-mannose required for a number of critical
CC mannosyl transfer reactions (By similarity).
CC -!- CATALYTIC ACTIVITY: D-mannose 6-phosphate = D-fructose 6-
CC phosphate.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-
CC phosphate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1
CC family.
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DR EMBL; AAFI02000070; EAL65112.1; -; Genomic_DNA.
DR RefSeq; XP_638475.1; XM_633383.1.
DR HSSP; P34948; 1PMI.
DR ProteinModelPortal; Q54PA0; -.
DR STRING; 44689.DDB_0231659; -.
DR EnsemblProtists; DDB0231659; DDB0231659; DDB_G0284685.
DR GeneID; 8624726; -.
DR KEGG; ddi:DDB_G0284685; -.
DR dictyBase; DDB_G0284685; mpi.
DR eggNOG; COG1482; -.
DR KO; K01809; -.
DR OMA; EMTIAIT; -.
DR ProtClustDB; CLSZ2497174; -.
DR UniPathway; UPA00126; UER00423.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004476; F:mannose-6-phosphate isomerase activity; ISS:dictyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009298; P:GDP-mannose biosynthetic process; ISS:dictyBase.
DR Gene3D; 2.60.120.10; -; 3.
DR InterPro; IPR001250; Man6P_Isoase-1.
DR InterPro; IPR016305; Mannose-6-P_Isomerase.
DR InterPro; IPR018050; Pmannose_isomerase-type1_CS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin.
DR PANTHER; PTHR10309; PTHR10309; 1.
DR Pfam; PF01238; PMI_typeI; 1.
DR PIRSF; PIRSF001480; Mannose-6-phosphate_isomerase; 1.
DR PRINTS; PR00714; MAN6PISMRASE.
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; 1.
PE 3: Inferred from homology;
KW Complete proteome; Cytoplasm; Isomerase; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1 452 Probable mannose-6-phosphate isomerase.
FT /FTId=PRO_0000327494.
FT COMPBIAS 3 20 Poly-Asn.
FT COMPBIAS 102 111 Poly-Ser.
FT ACT_SITE 314 314 By similarity.
FT METAL 141 141 Zinc (By similarity).
FT METAL 143 143 Zinc (By similarity).
FT METAL 168 168 Zinc (By similarity).
FT METAL 295 295 Zinc (By similarity).
SQ SEQUENCE 452 AA; 51091 MW; FBD259EF215E6D47 CRC64;
MENNNNNNNN NNNNNNNNNN IVLLKCVSQN YEWGKYGSNS TVAKLLKGYA KECSDIIKET
IPYAELWMGD HVSAPSKVEY KNKELKLREY IDTVQKEINE KSSTSSSSSS SIRGEIVEKR
FGNDFPFLFK VLSIRTALSI QAHPDSQLAQ VLFKKYPNIY KDPYHKPEIA IATTPFEALC
SFRPLSEIQS FIDTIPEFKN SLPNNLIKLD DCKEYLKSIV TSLLKADGLL ISNNLKELNN
RLNEKREEER DDLDRLVLKL YSQYPGDVGV FFAYILNYIV LKPGEALFLG AGEPHAYISG
DCVECMAPSD NVVRAGLTPK LKDVDTLGDM LTYRTGRPDL VVPQQRPDLS LTNYRCYQPP
VDEFQVEYYH LDDCCKNINV YSSKGPSIVL VYSGNLSIEN KSNQSTLNNL HTGSILFVPA
NTDYQFIQSD SSIPVSIYVA SVSNRIFNKN NL
//
