P37742 (RFBK7_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

Organism

Escherichia coli

Taxonomic identifier

562 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	453 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 O7 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
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 – 453	453	Phosphomannomutase		PRO_0000147823
Sites
	Active site	96	1	Phosphoserine intermediate By similarity
	Metal binding	96	1	Magnesium; via phosphate group By similarity
	Metal binding	243	1	Magnesium By similarity
	Metal binding	245	1	Magnesium By similarity
	Metal binding	247	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P37742 [UniParc]. Last modified October 1, 1994. Version 1. Checksum: F1D1F69F97804391	FASTA	453	49,932
	10 20 30 40 50 60 MLTCFKAYDI RGKLGEELNE DIAWRIGRAY GEFLKPKTIV LGGDVRLTSE TLKLALAKGL 70 80 90 100 110 120 QDAGVDVLDI GMSGTEEIYF ATFHLGVDGG IEVTASHNPM DYNGMKLVRE GARPISGDTG 130 140 150 160 170 180 LRDVQRLAEA NDFPPVDETK RGRYQQINLR DAYVDHLFGY INVKNLTPLK LVINSGNGAA 190 200 210 220 230 240 GPVVDAIEAR FKALGAPVEL IKVHNTPDGN FPNGIPNPLL PECRDDTRNA VIKHGADMGI 250 260 270 280 290 300 AFDGDFDRCF LFDEKGQFIE GYYIVGLLAE AFLEKNPGAK IIHDPRLSWN TVDVVTAAGT 310 320 330 340 350 360 PVMSKTGHAF IKERMRKEDA IYGGEMSAHH YFRDFAYCDT GMIPWLLVAE LVCLKGKTLG 370 380 390 400 410 420 ELVRDRMAAF PASGEINSKL AHPVEAINRV EQHFSRDAGG GSHRWHQHDL CRLAALTCAS 430 440 450 SNTEPVVRLN VESRGDVPLM EEKTKLILEL LNK

References

[1]

"Identification, expression, and DNA sequence of the GDP-mannose biosynthesis genes encoded by the O7 rfb gene cluster of strain VW187 (Escherichia coli O7:K1)." Marolda C.L., Valvano M.A. J. Bacteriol. 175:148-158(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: O7:K1 / VW187.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF125322 Genomic DNA. Translation: AAC27539.1. Sequence problems.
PIR	D40630.
3D structure databases
ProteinModelPortal	P37742.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG1109.
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. 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. [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

RFBK7_ECOLX

Accession

Primary (citable) accession number: P37742

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	October 1, 1994
Last modified:	April 3, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program