O85342 (MANC2_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannose-1-phosphate guanylyltransferase 2
EC=2.7.7.13

Alternative name(s):
GDP-mannose pyrophosphorylase 2
Short name=GMP 2
Short name=GMPP 2

Gene names

Name:	manC2
Synonyms:	manC
Ordered Locus Names:	Z3195, ECs2836

Organism

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

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	482 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. Ref.1
Catalytic activity	GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose.
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate (GTP route): step 1/1.
Sequence similarities	Belongs to the mannose-6-phosphate isomerase type 2 family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Ligand	GTP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW mannose-1-phosphate guanylyltransferase 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 – 482	482	Mannose-1-phosphate guanylyltransferase 2		PRO_0000194254

Sequences

	Sequence		Length	Mass (Da)
	O85342 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 0BB237825F6C4614	FASTA	482	54,270
	10 20 30 40 50 60 MSDAPIIAVV MAGGTGSRLW PLSRELYPKQ FLQLSGDNTL LQTTLLRLSG LSCQKPLVIT 70 80 90 100 110 120 NEQHRFVVAE QLREINKLNG NIILEPCGRN TAPAIAISAF HALKRNPQED PLLLVLAADH 130 140 150 160 170 180 VIAKESVFCD AIKNATPIAN QGKIVTFGII PEYAETGYGY IERGELSVPL QGHENTGFYY 190 200 210 220 230 240 VNKFVEKPNR ETAELYMTSG NHYWNSGIFM FKASVYLEEL RKFRPDIYNV CEQVASSSYI 250 260 270 280 290 300 DLDFIRLSKE QFQDCPAESI DFAVMEKTEK CVVCPVDIGW SDVGSWQSLW DISLKSKTGD 310 320 330 340 350 360 VCKGDILTYD TKNNYIYSES ALVAAIGIED MVIVQTKDAV LVSKKSDVQH VKKIVEMLKL 370 380 390 400 410 420 QQRTEYISHR EVFRPWGKFD SIDQGERYKV KKIIVKPGEG LSLRMHHHRS EHWIVLSGTA 430 440 450 460 470 480 KVTLGDKTKL VTANESIYIP LGAAYSLENP GIIPLNLIEV SSGDYLGEDD IIRQKERYKH ED

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: 9673232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: O157:H7 / C664-1992 / EHEC.
[2]	"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: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[3]	"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: 11258796] [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: AAC32348.1. AE005174 Genomic DNA. Translation: AAG57091.1. BA000007 Genomic DNA. Translation: BAB36259.1.
PIR	D90983. G85828.
RefSeq	NP_288537.1. NC_002655.2. NP_310863.1. NC_002695.1.
3D structure databases
ProteinModelPortal	O85342.
SMR	O85342. Positions 5-360, 375-465.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000026104; EBESCP00000024997; EBESCG00000025157. EBESCT00000056802; EBESCP00000054630; EBESCG00000055850.
GeneID	912820. 962090.
GenomeReviews	Gene locus Z3195 in contig AE005174_GR. Gene locus ECs2836 in contig BA000007_GR.
KEGG	ece:Z3195. ecs:ECs2836.
PATRIC	18355056. VBIEscCol44059_2729.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000011908.
HOGENOM	HBG422488.
OMA	DKNKDQE.
ProtClustDB	CLSK334800.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS2836-MONOMER.
Family and domain databases
InterPro	IPR011051. Cupin_RmlC_type. IPR006375. Man1P_GuaTrfase/Man6P_Isoase. IPR001538. Man6P_isomerase-2_C. IPR005835. NTP_transferase. IPR014710. RmlC-like_jellyroll. [Graphical view]
Gene3D	G3DSA:2.60.120.10. RmlC-like_jellyroll. 1 hit.
KO	K00971.
Pfam	PF01050. MannoseP_isomer. 1 hit. PF00483. NTP_transferase. 1 hit. [Graphical view]
SUPFAM	SSF51182. RmlC_like_cupin. 1 hit.
TIGRFAMs	TIGR01479. GMP_PMI. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MANC2_ECO57

Accession

Primary (citable) accession number: O85342

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	November 1, 1998
Last modified:	January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program