Mannose-6-phosphate isomerase - Escherichia coli (strain K12)

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P00946 (MANA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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
Synonyms:	pmi
Ordered Locus Names:	b1613, JW1605

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	391 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the conversion of glucose to GDP-L-fucose, which can be converted to L-fucose, a capsular polysaccharide.
Catalytic activity	D-mannose 6-phosphate = D-fructose 6-phosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
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
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from mutant phenotype PubMed 4862193. Source: EcoCyc colanic acid biosynthetic process Inferred from mutant phenotype PubMed 4862193. Source: EcoCyc mannose catabolic process Inferred from mutant phenotype PubMed 4862193. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mannose-6-phosphate isomerase activity Inferred from direct assay PubMed 5335965. Source: EcoCyc 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 – 391

391

Mannose-6-phosphate isomerase

PRO_0000194230

Sites

Active site

274

By similarity

Metal binding

Zinc By similarity

Metal binding

Zinc By similarity

Metal binding

134

Zinc By similarity

Metal binding

255

Zinc By similarity

Amino acid modifications

Modified residue

280

N6-acetyllysine Ref.6

Sequences

Sequence

Length

Mass (Da)

Tools

P00946 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 669737512CADBCCD
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FASTA

391

42,850

        10         20         30         40         50         60 
MQKLINSVQN YAWGSKTALT ELYGMENPSS QPMAELWMGA HPKSSSRVQN AAGDIVSLRD 

        70         80         90        100        110        120 
VIESDKSTLL GEAVAKRFGE LPFLFKVLCA AQPLSIQVHP NKHNSEIGFA KENAAGIPMD 

       130        140        150        160        170        180 
AAERNYKDPN HKPELVFALT PFLAMNAFRE FSEIVSLLQP VAGAHPAIAH FLQQPDAERL 

       190        200        210        220        230        240 
SELFASLLNM QGEEKSRALA ILKSALDSQQ GEPWQTIRLI SEFYPEDSGL FSPLLLNVVK 

       250        260        270        280        290        300 
LNPGEAMFLF AETPHAYLQG VALEVMANSD NVLRAGLTPK YIDIPELVAN VKFEAKPANQ 

       310        320        330        340        350        360 
LLTQPVKQGA ELDFPIPVDD FAFSLHDLSD KETTISQQSA AILFCVEGDA TLWKGSQQLQ 

       370        380        390 
LKPGESAFIA ANESPVTVKG HGRLARVYNK L

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and transcriptional start point of the phosphomannose isomerase gene (manA) of Escherichia coli." Miles J.S., Guest J.R. Gene 32:41-48(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	Robison K., O'Keeffe T., Church G.M. Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 378-391. Strain: K12 / EMG2.
[6]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M15380 Genomic DNA. Translation: AAA24109.1. U00096 Genomic DNA. Translation: AAC74685.1. AP009048 Genomic DNA. Translation: BAA15361.1. U35067 Genomic DNA. Translation: AAA79050.1.
PIR	ISECMP. A01172.
RefSeq	NP_416130.3. NC_000913.2. YP_489876.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P00946.
SMR	P00946. Positions 1-391.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10153N.
IntAct	P00946. 19 interactions.
MINT	MINT-1241491.
STRING	511145.b1613.
2D gel databases
SWISS-2DPAGE	P00946.
Proteomic databases
PaxDb	P00946.
PRIDE	P00946.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74685; AAC74685; b1613. BAA15361; BAA15361; BAA15361.
GeneID	12931261. 944840.
KEGG	ecj:Y75_p1589. eco:b1613.
PATRIC	32118528. VBIEscCol129921_1684.
Organism-specific databases
EchoBASE	EB0561.
EcoGene	EG10566. manA.
Phylogenomic databases
eggNOG	COG1482.
HOGENOM	HOG000241278.
KO	K01809.
OMA	VMKMEVP.
ProtClustDB	PRK15131.
Enzyme and pathway databases
BioCyc	EcoCyc:MANNPISOM-MONOMER. ECOL316407:JW1605-MONOMER. MetaCyc:MANNPISOM-MONOMER.
Gene expression databases
Genevestigator	P00946.
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

MANA_ECOLI

Accession

Primary (citable) accession number: P00946

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents