P54746 (MNGB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannosylglycerate hydrolase
EC=3.2.1.170

Alternative name(s):
2-O-(6-phospho-mannosyl)-D-glycerate hydrolase
Alpha-mannosidase mngB

Gene names

Name:	mngB
Synonyms:	ybgG
Ordered Locus Names:	b0732, JW0721

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	877 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May hydrolyze mannosyl-D-glycerate to mannose-6-phosphate and glycerate. Ref.5
Catalytic activity	2-O-(6-phospho-alpha-D-mannosyl)-D-glycerate + H2O = D-mannose 6-phosphate + D-glycerate. Ref.5
Cofactor	Binds one divalent metal cation per subunit By similarity.
Induction	Repressed by MngR. Induced by mannosyl-D-glycerate.
Sequence similarities	Belongs to the glycosyl hydrolase 38 family.

Ontologies

Keywords
Ligand	Metal-binding
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mannose metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	alpha-mannosidase activity Inferred from mutant phenotype Ref.5. Source: EcoliWiki carbohydrate binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 877	877	Mannosylglycerate hydrolase		PRO_0000168700
Sites
	Active site	126	1	Nucleophile By similarity
	Metal binding	14	1	Divalent metal cation By similarity
	Metal binding	16	1	Divalent metal cation By similarity
	Metal binding	126	1	Divalent metal cation By similarity
	Metal binding	338	1	Divalent metal cation By similarity
Experimental info
	Sequence conflict	87 – 100	14	WYTQT…VSAES → GIPRPIPRLFCGNP Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P54746 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: B67201C6F8CB1C0A	FASTA	877	100,015
	10 20 30 40 50 60 MKAVSRVHIT PHMHWDREWY FTTEESRILL VNNMEEILCR LEQDNEYKYY VLDGQTAILE 70 80 90 100 110 120 DYFAVKPENK DRVKKQVEAG KLIIGPWYTQ TDTTIVSAES IVRNLMYGMR DCLAFGEPMK 130 140 150 160 170 180 IGYLPDSFGM SGQLPHIYNG FGITRTMFWR GCSERHGTDK TEFLWQSSDG SEVTAQVLPL 190 200 210 220 230 240 GYAIGKYLPA DENGLRKRLD SYFDVLEKAS VTKEILLPNG HDQMPLQQNI FEVMDKLREI 250 260 270 280 290 300 YPQRKFVMSR FEEVFEKIEA QRDNLATLKG EFIDGKYMRV HRTIGSTRMD IKIAHARIEN 310 320 330 340 350 360 KIVNLLEPLA TLAWTLGFEY HHGLLEKMWK EILKNHAHDS IGCCCSDKVH REIVARFELA 370 380 390 400 410 420 EDMADNLIRF YMRKIADNMP QSDADKLVLF NLMPWPREEV INTTVRLRAS QFNLRDDRGQ 430 440 450 460 470 480 PVPYFIRHAR EIDPGLIDRQ IVHYGNYDPF MEFDIQINQI VPSMGYRTLY IEANQPGNVI 490 500 510 520 530 540 AAKSDAEGIL ENAFWQIALN EDGSLQLVDK DSGVRYDRVL QIEESSDDGD EYDYSPAKEE 550 560 570 580 590 600 WVITAANAKP QCDIIHEAWQ SRAVIRYDMA VPLNLSERSA RQSTGRVGVV LVVTLSHNSR 610 620 630 640 650 660 RIDVDINLDN QADDHRLRVL VPTPFNTDSV LADTQFGSLT RPVNDSAMNN WQQEGWKEAP 670 680 690 700 710 720 VPVWNMLNYV ALQEGRNGMA VFSEGLREFE VIGEEKKTFA ITLLRGVGLL GKEDLLLRPG 730 740 750 760 770 780 RPSGIKMPVP DSQLRGLLSC RLSLLSYTGT PTAAGVAQQA RAWLTPVQCY NKIPWDVMKL 790 800 810 820 830 840 NKAGFNVPES YSLLKMPPVG CLISALKKAE DRQEVILRLF NPAESATCDA TVAFSREVIS 850 860 870 CSETMMDEHI TTEENQGSNL SGPFLPGQSR TFSYRLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"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.
[3]	"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.
[4]	"Isolation and characterization of the heat-responsive genes in Escherichia coli." Utsumi R., Horie T., Katoh A., Kaino Y., Tanabe H., Noda M. Biosci. Biotechnol. Biochem. 60:309-315(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
[5]	"Phosphotransferase-mediated transport of the osmolyte 2-O-alpha-mannosyl-D-glycerate in Escherichia coli occurs by the product of the mngA (hrsA) gene and is regulated by the mngR (farR) gene product acting as repressor." Sampaio M.-M., Chevance F., Dippel R., Eppler T., Schlegel A., Boos W., Lu Y.-J., Rock C.O. J. Biol. Chem. 279:5537-5548(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A MANNOSIDASE, CATALYTIC ACTIVITY. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC73826.1. AP009048 Genomic DNA. Translation: BAA35398.1. D64014 Genomic DNA. No translation available.
PIR	C64809.
RefSeq	NP_415260.1. NC_000913.2. YP_489011.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P54746.
ModBase	Search...
Protein-protein interaction databases
IntAct	P54746. 14 interactions.
STRING	511145.b0732.
Protein family/group databases
CAZy	GH38. Glycoside Hydrolase Family 38.
Proteomic databases
PaxDb	P54746.
PRIDE	P54746.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73826; AAC73826; b0732. BAA35398; BAA35398; BAA35398.
GeneID	12934548. 945359.
KEGG	ecj:Y75_p0711. eco:b0732.
PATRIC	32116659. VBIEscCol129921_0762.
Organism-specific databases
EchoBASE	EB3025.
EcoGene	EG13236. mngB.
Phylogenomic databases
eggNOG	COG0383.
HOGENOM	HOG000231434.
KO	K15524.
OMA	IRYEMAV.
ProtClustDB	PRK09819.
Enzyme and pathway databases
BioCyc	EcoCyc:EG13236-MONOMER. ECOL316407:JW0721-MONOMER. MetaCyc:EG13236-MONOMER.
Gene expression databases
Genevestigator	P54746.
Family and domain databases
Gene3D	3.20.110.10. 1 hit.
InterPro	IPR011013. Gal_mutarotase_SF_dom. IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR027291. Glyco_hydro_38/57_N. IPR011682. Glyco_hydro_38_C. IPR015341. Glyco_hydro_38_cen_dom. IPR000602. Glyco_hydro_38_N. [Graphical view]
Pfam	PF09261. Alpha-mann_mid. 1 hit. PF01074. Glyco_hydro_38. 1 hit. PF07748. Glyco_hydro_38C. 1 hit. [Graphical view]
SMART	SM00872. Alpha-mann_mid. 1 hit. [Graphical view]
SUPFAM	SSF74650. Gal_mut_like. 1 hit. SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MNGB_ECOLI

Accession

Primary (citable) accession number: P54746
Secondary accession number(s): P75753

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program