Reviewed, UniProtKB/Swiss-Prot P00946 (MANA_ECOLI)

Names and origin

Protein names

Recommended name:
    Mannose-6-phosphate isomerase
    EC=5.3.1.8
Alternative name(s):
    Phosphomannose isomerase
      Short name=PMI
    Phosphohexomutase

Gene names

Name:	manA
Synonyms:	pmi
Ordered Locus Names:	b1613, JW1605

Organism

Escherichia coli (strain K12) [Complete 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
Gene Ontology (GO)
Biological process	GDP-mannose biosynthetic process Inferred from mutant phenotype. Source: UniProtKB colanic acid biosynthetic process Inferred from mutant phenotype. Source: UniProtKB mannose catabolic process Inferred from mutant phenotype. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	mannose-6-phosphate isomerase activity Inferred from direct assay. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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	1	By similarity
	Metal binding	97	1	Zinc By similarity
	Metal binding	99	1	Zinc By similarity
	Metal binding	134	1	Zinc By similarity
	Metal binding	255	1	Zinc By similarity
Amino acid modifications
	Modified residue	280	1	N6-acetyllysine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P00946-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 669737512CADBCCD	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

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: 6397402] [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. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [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: 9278503] [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: 16738553] [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: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, MASS SPECTROMETRY.

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	AP_002234.1. NP_416130.3.
3D structure databases
SMR	P00946. Positions 1-382.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10153N.
STRING	P00946.
2-D gel databases
SWISS-2DPAGE	P00946.
Genome annotation databases
GeneID	944840.
GenomeReviews	Gene locus JW1605 in contig AP009048_GR. Gene locus b1613 in contig U00096_GR.
KEGG	ecj:JW1605. eco:b1613.
Organism-specific databases
EchoBASE	EB0561.
EcoGene	EG10566. manA.
CMR	Search...
Phylogenomic databases
eggNOG	COG1482.
HOGENOM	HBG590632.
OMA	DFTVMKM.
Enzyme and pathway databases
BioCyc	EcoCyc:MANNPISOM-MONOMER. ECOL168927:B1613-MONOMER. MetaCyc:MANNPISOM-MONOMER.
Gene expression databases
Genevestigator	P00946.
Family and domain databases
InterPro	IPR011051. Cupin_RmlC_type. IPR001250. Man6P_Isoase-1. IPR016305. Mannose-6-P_Isomerase. IPR018050. Pmannose_isomerase-type1_CS. IPR014710. RmlC-like_jellyroll. [Graphical view]
Gene3D	G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
Pfam	PF01238. PMI_typeI. 1 hit. [Graphical view]
PIRSF	PIRSF001480. Mannose-6-phosphate_isomerase. 1 hit.
PRINTS	PR00714. MAN6PISMRASE.
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:	February 9, 2010
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)