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Database: UniProt
Entry: P29951
LinkDB: P29951
Original site: P29951 
ID   MPI_EMENI               Reviewed;         461 AA.
AC   P29951; C8VRS9; Q5BFL3;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   26-NOV-2014, entry version 103.
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=manA; ORFNames=AN0667;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8307007; DOI=10.1111/j.1432-1033.1994.tb19954.x;
RA   Proudfoot A.E.I., Turcatti G., Wells T.N.C., Payton M.A., Smith D.J.;
RT   "Purification, cDNA cloning and heterologous expression of human
RT   phosphomannose isomerase.";
RL   Eur. J. Biochem. 219:415-423(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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.
CC   -!- CATALYTIC ACTIVITY: D-mannose 6-phosphate = D-fructose 6-
CC       phosphate.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the mannose-6-phosphate isomerase type 1
CC       family. {ECO:0000305}.
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DR   EMBL; M85239; AAA33319.1; -; Genomic_DNA.
DR   EMBL; AACD01000010; EAA65443.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF89025.1; -; Genomic_DNA.
DR   PIR; A56239; A56239.
DR   RefSeq; XP_658271.1; XM_653179.1.
DR   ProteinModelPortal; P29951; -.
DR   STRING; 162425.CADANIAP00002007; -.
DR   EnsemblFungi; CADANIAT00002007; CADANIAP00002007; CADANIAG00002007.
DR   GeneID; 2876445; -.
DR   KEGG; ani:AN0667.2; -.
DR   eggNOG; COG1482; -.
DR   HOGENOM; HOG000241277; -.
DR   InParanoid; P29951; -.
DR   KO; K01809; -.
DR   OMA; PYAEFWV; -.
DR   UniPathway; UPA00126; UER00423.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004476; F:mannose-6-phosphate isomerase activity; ISS:ASPGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000032; P:cell wall mannoprotein biosynthetic process; ISS:ASPGD.
DR   GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0030448; P:hyphal growth; IMP:ASPGD.
DR   GO; GO:0006486; P:protein glycosylation; ISS:ASPGD.
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; SSF51182; 1.
DR   TIGRFAMs; TIGR00218; manA; 1.
DR   PROSITE; PS00965; PMI_I_1; 1.
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    461       Mannose-6-phosphate isomerase.
FT                                /FTId=PRO_0000194244.
FT   ACT_SITE    310    310       {ECO:0000250}.
FT   METAL       107    107       Zinc. {ECO:0000250}.
FT   METAL       109    109       Zinc. {ECO:0000250}.
FT   METAL       134    134       Zinc. {ECO:0000250}.
FT   METAL       291    291       Zinc. {ECO:0000250}.
FT   CONFLICT     19     19       R -> K (in Ref. 1; AAA33319).
FT                                {ECO:0000305}.
SQ   SEQUENCE   461 AA;  50613 MW;  17E0D089A6656F79 CRC64;
     MQVPLLRLQC GVNSYDWGRV GPESAAAKYA AATAPSDFTI EADKPYAELW MGTHPSLPSK
     DVETQRTLLD MVQDNLALMS PEVSERYGGK LPFLFKVLSI RKALSIQAHP NKKLAEALHA
     RDPRNYPDDN HKPEMTIAIT PFEGLCGFRP LAEIVHFLKA VAPLRYLIGV QTATDFENAV
     RGFENTEDPE QTKKNKVALR TLFTSLMQSA SENIEQAARE LVAAAQSSPE TFASLVNAPD
     TNPTNAAELA SIIIRLNEQF PNDIGLFVFF FLNFVRLEPG EAMFLKADDI HAYISGDIIE
     CMASSDNVVR AGFTPKFKDV DTLTEMLTYS YAPIDEQKLQ PTDYPYTVLN AAAYSSASDS
     LLYDPPIEEF SVVKTSLRRT GAKATFDPLT GPSILICTGG TGKISVGHKT EEVKEGYVFF
     VGANAECIIE NTGTGSDEEN VFTTFKAFCD LTGKEDMANG H
//
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