P29951 (MPI_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannose-6-phosphate isomerase
EC=5.3.1.8

Alternative name(s):
Phosphohexomutase
Phosphomannose isomerase
Short name=PMI

Gene names

Name:	manA
ORF Names:	AN0667

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella › Emericella nidulans › mitosporic Emericella nidulans

Protein attributes

Sequence length	461 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Catalytic activity	D-mannose 6-phosphate = D-fructose 6-phosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 1/2.
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the mannose-6-phosphate isomerase type 1 family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mannose-6-phosphate isomerase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 461	461	Mannose-6-phosphate isomerase		PRO_0000194244
Sites
	Active site	310	1	By similarity
	Metal binding	107	1	Zinc By similarity
	Metal binding	109	1	Zinc By similarity
	Metal binding	134	1	Zinc By similarity
	Metal binding	291	1	Zinc By similarity
Experimental info
	Sequence conflict	19	1	R → K in AAA33319. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P29951 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 17E0D089A6656F79	FASTA	461	50,613
	10 20 30 40 50 60 MQVPLLRLQC GVNSYDWGRV GPESAAAKYA AATAPSDFTI EADKPYAELW MGTHPSLPSK 70 80 90 100 110 120 DVETQRTLLD MVQDNLALMS PEVSERYGGK LPFLFKVLSI RKALSIQAHP NKKLAEALHA 130 140 150 160 170 180 RDPRNYPDDN HKPEMTIAIT PFEGLCGFRP LAEIVHFLKA VAPLRYLIGV QTATDFENAV 190 200 210 220 230 240 RGFENTEDPE QTKKNKVALR TLFTSLMQSA SENIEQAARE LVAAAQSSPE TFASLVNAPD 250 260 270 280 290 300 TNPTNAAELA SIIIRLNEQF PNDIGLFVFF FLNFVRLEPG EAMFLKADDI HAYISGDIIE 310 320 330 340 350 360 CMASSDNVVR AGFTPKFKDV DTLTEMLTYS YAPIDEQKLQ PTDYPYTVLN AAAYSSASDS 370 380 390 400 410 420 LLYDPPIEEF SVVKTSLRRT GAKATFDPLT GPSILICTGG TGKISVGHKT EEVKEGYVFF 430 440 450 460 VGANAECIIE NTGTGSDEEN VFTTFKAFCD LTGKEDMANG H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification, cDNA cloning and heterologous expression of human phosphomannose isomerase." Proudfoot A.E.I., Turcatti G., Wells T.N.C., Payton M.A., Smith D.J. Eur. J. Biochem. 219:415-423(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M85239 Genomic DNA. Translation: AAA33319.1. AACD01000010 Genomic DNA. Translation: EAA65443.1. BN001308 Genomic DNA. Translation: CBF89025.1.
PIR	A56239.
RefSeq	XP_658271.1. XM_653179.1.
3D structure databases
ProteinModelPortal	P29951.
ModBase	Search...
Protein-protein interaction databases
STRING	162425.CADANIAP00002007.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00002007; CADANIAP00002007; CADANIAG00002007.
GeneID	2876445.
KEGG	ani:AN0667.2.
Phylogenomic databases
eggNOG	COG1482.
HOGENOM	HOG000241277.
KO	K01809.
OMA	EMTIAIT.
OrthoDB	EOG4TF3V5.
Enzyme and pathway databases
UniPathway	UPA00126; UER00423.
Family and domain databases
Gene3D	2.60.120.10. 3 hits.
InterPro	IPR001250. Man6P_Isoase-1. IPR016305. Mannose-6-P_Isomerase. IPR018050. Pmannose_isomerase-type1_CS. IPR014710. RmlC-like_jellyroll. IPR011051. RmlC_Cupin. [Graphical view]
PANTHER	PTHR10309. PTHR10309. 1 hit.
Pfam	PF01238. PMI_typeI. 1 hit. [Graphical view]
PIRSF	PIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTS	PR00714. MAN6PISMRASE.
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMs	TIGR00218. manA. 1 hit.
PROSITE	PS00965. PMI_I_1. 1 hit. PS00966. PMI_I_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MPI_EMENI

Accession

Primary (citable) accession number: P29951
Secondary accession number(s): C8VRS9, Q5BFL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	May 1, 2007
Last modified:	April 3, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program