O85343 (MANB_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphomannomutase
Short name=PMM
EC=5.4.2.8

Gene names

Name:	manB
Ordered Locus Names:	Z3194, ECs2835

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [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 GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS O antigen.
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. Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	GDP-mannose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway O antigen biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
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_0000147819
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)
	O85343 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 6845D9D2DD7628B7	FASTA	456	50,340
	10 20 30 40 50 60 MKSLTCFKAY DIRGKLGEEL NEDIAWRIGR AYGEFLKPKT IVLGGDVRLT SEALKLALAK 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 VAELVCLKGK 370 380 390 400 410 420 TLGEMVRDRM AAFPASGEIN SKLAQPVEAI NRVEQHFSRE ALAVDRTDGI SMTFADWRFN 430 440 450 LRSSNTEPVV RLNVESRGDV KLMEKKTKAL LKLLSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization of Escherichia coli O157 O antigen gene cluster and identification of its specific genes." Wang L., Reeves P.R. Infect. Immun. 66:3545-3551(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O157:H7 / C664-1992 / EHEC.
[2]	"Analysis of the genes responsible for the O-antigen synthesis in enterohaemorrhagic Escherichia coli O157." Shimizu T., Yamasaki S., Tsukamoto T., Takeda Y. Microb. Pathog. 26:235-247(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O157:H- / 184 / EHEC.
[3]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[4]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF061251 Genomic DNA. Translation: AAC32349.1. AB008676 Genomic DNA. Translation: BAA77734.1. AE005174 Genomic DNA. Translation: AAG57090.1. BA000007 Genomic DNA. Translation: BAB36258.1.
PIR	C90983. F85828.
RefSeq	NP_288536.1. NC_002655.2. NP_310862.1. NC_002695.1.
3D structure databases
ProteinModelPortal	O85343.
SMR	O85343. Positions 1-456.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z3194.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG57090; AAG57090; Z3194. BAB36258; BAB36258; BAB36258.
GeneID	913941. 962089.
KEGG	ece:Z3194. ecs:ECs2835.
PATRIC	18355054. VBIEscCol44059_2728.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1109.
HOGENOM	HOG000268679.
KO	K01840.
OMA	MNNLTCF.
ProtClustDB	PRK15414.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-2797-MONOMER.
UniPathway	UPA00126; UER00424. UPA00281.
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_ECO57

Accession

Primary (citable) accession number: O85343

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program