P24175 (MANB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphomannomutase
Short name=PMM
EC=5.4.2.8

Gene names

Name:	manB
Synonyms:	cpsG, rfbL
Ordered Locus Names:	b2048, JW2033

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in the biosynthesis of the capsular polysaccharide colanic acid.
Catalytic activity	Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Cofactor	Binds 1 magnesium 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 2/2.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Capsule biogenesis/degradation Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphomannomutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 456	456	Phosphomannomutase		PRO_0000147818
Sites
	Active site	98	1	Phosphoserine intermediate By similarity
	Metal binding	98	1	Magnesium; via phosphate group By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	247	1	Magnesium By similarity
	Metal binding	249	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P24175 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 8A96663D7A60BFD1	FASTA	456	50,463
	10 20 30 40 50 60 MKKLTCFKAY DIRGKLGEEL NEDIAWRIGR AYGEFLKPKT IVLGGDVRLT SETLKLALAK 70 80 90 100 110 120 GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN PMDYNGMKLV REGARPISGD 130 140 150 160 170 180 TGLRDVQRLA EANDFPPVDE TKRGRYQQIN LRDAYVDHLF GYINVKNLTP LKLVINSGNG 190 200 210 220 230 240 AAGPVVDAIE ARFKALGAPV ELIKVHNTPD GNFPNGIPNP LLPECRDDTR NAVIKHGADM 250 260 270 280 290 300 GIAFDGDFDR CFLFDEKGQF IEGYYIVGLL AEAFLEKNPG AKIIHDPRLS WNTVDVVTAA 310 320 330 340 350 360 GGTPVMSKTG HAFIKERMRK EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL VAELVCLKDK 370 380 390 400 410 420 TLGELVRDRM AAFPASGEIN SKLAQPVEAI NRVEQHFSRE ALAVDRTDGI SMTFADWRFN 430 440 450 LRTSNTEPVV RLNVESRGDV PLMEARTRTL LTLLNE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of the phosphoglucomutase gene in E. coli." Tal R., Eichinger G., Emerick A., Wong H.C. Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Evidence for effect of random genetic drift on G+C content after lateral transfer of fucose pathway genes to Escherichia coli K-12." Aoyama K., Haase A.M., Reeves P.R. Mol. Biol. Evol. 11:829-838(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid." Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R. J. Bacteriol. 178:4885-4893(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[4]	"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., 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., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"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.
[6]	"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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M77127 Genomic DNA. Translation: AAA02894.1. U38473 Genomic DNA. Translation: AAC77847.1. U00096 Genomic DNA. Translation: AAC75109.1. AP009048 Genomic DNA. Translation: BAA15901.1.
PIR	B55239.
RefSeq	NP_416552.1. NC_000913.2. YP_490290.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P24175.
SMR	P24175. Positions 1-442.
ModBase	Search...
Protein-protein interaction databases
IntAct	P24175. 9 interactions.
STRING	511145.b2048.
Proteomic databases
PRIDE	P24175.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75109; AAC75109; b2048. BAA15901; BAA15901; BAA15901.
GeneID	12934315. 946574.
KEGG	ecj:Y75_p2011. eco:b2048.
PATRIC	32119429. VBIEscCol129921_2125.
Organism-specific databases
EchoBASE	EB0160.
EcoGene	EG10162. manB.
Phylogenomic databases
HOGENOM	HOG000268679.
KO	K01840.
OMA	RDAYIGH.
ProtClustDB	PRK15414.
Enzyme and pathway databases
BioCyc	EcoCyc:PHOSMANMUT-MONOMER. ECOL316407:JW2033-MONOMER. MetaCyc:PHOSMANMUT-MONOMER.
UniPathway	UPA00126; UER00424.
Gene expression databases
Genevestigator	P24175.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. [Graphical view]
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANB_ECOLI

Accession

Primary (citable) accession number: P24175

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 1992
Last sequence update:	March 1, 1992
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program