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 03-APR-2013, entry version 96.
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; Trichocomaceae; Emericella.
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: 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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 KO; K01809; -.
DR OMA; EMTIAIT; -.
DR OrthoDB; EOG4TF3V5; -.
DR UniPathway; UPA00126; UER00423.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 GO; GO:0009298; P:GDP-mannose biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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 By similarity.
FT METAL 107 107 Zinc (By similarity).
FT METAL 109 109 Zinc (By similarity).
FT METAL 134 134 Zinc (By similarity).
FT METAL 291 291 Zinc (By similarity).
FT CONFLICT 19 19 R -> K (in Ref. 1; AAA33319).
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
//
