P37755 (RFBK9_ECOLX) 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:	rfbK, rfbK2

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

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

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 O9 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.
Miscellaneous	There are two duplicated genes for manB and manC in this E.coli strain.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
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_0000147824
Sites
	Active site	98	1	Phosphoserine intermediate By similarity
	Metal binding	98	1	Magnesium; via phosphate group By similarity
	Metal binding	246	1	Magnesium By similarity
	Metal binding	248	1	Magnesium By similarity
	Metal binding	250	1	Magnesium By similarity
Natural variations
	Natural variant	392	1	A → R.
	Natural variant	441	1	T → V.
	Natural variant	446	1	A → E.
	Natural variant	449 – 453	5	EEILA → TELLN.
	Natural variant	456	1	K → KEELL.

Sequences

	Sequence		Length	Mass (Da)
	P37755 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: 40100B6075791BF3	FASTA	456	50,423
	10 20 30 40 50 60 MTQLTCFKAY DIRGELGEEL NEDIAYRIGR AYGEFLKPGK IVVGGDVRLT SESLKLALAR 70 80 90 100 110 120 GLMDAGTDVL DIGLSGTEEI YFATFHLGVD GGIEVTASHN PMNYNGMKLV RENAKPISGD 130 140 150 160 170 180 TGLRDIQRLA EENQFPPVDP ARRGTLRQIS VLKEYVDHLM GYVDLANFTR PLKLVVNSGN 190 200 210 220 230 240 GAAGHVIDEV EKRFAAAGVP VTFIKVHHQP DGHFPNGIPN PLLPECRQDT ADAVREHQAD 250 260 270 280 290 300 MGIAFDGDFD RCFLFDDEAS FIEGYYIVGL LAEAFLQKQP GAKIIHDPRL TWNTVDIVTR 310 320 330 340 350 360 NGGQPVMSKT GHAFIKERMR QEDAIYGGEM SAHHYFRDFA YCDSGMIPWL LVAELLCLKN 370 380 390 400 410 420 SSLKSLVADR QAAFPASGEI NRKLGNAAEA IARIRAQYEP AAAHIDTTDG ISIEYPEWRF 430 440 450 NLRTSNTEPV VRLNVESRAD TALMNAKTEE ILALLK

References

[1]

"Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli O9:K30 and participation of rfb genes in the synthesis of the group I K30 capsular polysaccharide." Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., Whitfield C. J. Bacteriol. 176:3126-3139(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O9:K30:H12 / E69.

[2]

"Bacterial polysaccharide synthesis and gene nomenclature." Reeves P.R., Hobbs M., Valvano M.A., Skurnik M., Whitfield C., Coplin D., Kido N., Klena J., Maskell D., Raetz C.R.H., Rick P.D. Trends Microbiol. 4:495-503(1996) [PubMed] [Europe PMC] [Abstract] Cited for: GENE NAME.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L27646 Genomic DNA. Translation: AAA21138.1. L27632 Genomic DNA. Translation: AAA21140.1.
3D structure databases
ProteinModelPortal	P37755.
ModBase	Search...
Proteomic databases
PRIDE	P37755.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
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

RFBK9_ECOLX

Accession

Primary (citable) accession number: P37755
Secondary accession number(s): P82275

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program