Reviewed, UniProtKB/Swiss-Prot O85713 (NOEL_RHIFR)

Names and origin

Protein names

Recommended name:
    GDP-mannose 4,6-dehydratase
    EC=4.2.1.47
Alternative name(s):
    GDP-D-mannose dehydratase

Gene names

Name:

noeL

Encoded on

Plasmid pSfHH103d

Organism

Rhizobium fredii (Sinorhizobium fredii)

Taxonomic identifier

380 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose + H2O.
Cofactor	NAD.
Pathway	Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.
Sequence similarities	Belongs to the GDP-mannose 4,6-dehydratase family.

Ontologies

Keywords
Biological process	Nodulation
Ligand	NAD
Molecular function	Lyase
Technical term	Plasmid
Gene Ontology (GO)
Biological process	GDP-mannose metabolic process Inferred from electronic annotation. Source: InterPro nodulation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	GDP-mannose 4,6-dehydratase activity Inferred from electronic annotation. Source: EC coenzyme 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 – 351	351	GDP-mannose 4,6-dehydratase		PRO_0000201720
Sites
	Active site	135	1	By similarity
	Active site	137	1	Nucleophile By similarity
	Active site	159	1	Nucleophile By similarity
	Binding site	163	1	NADP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O85713-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 0E6A32874B3061EB	FASTA	351	40,014
	10 20 30 40 50 60 MTDRKVALIS GVTGQDGAYL AELLLDEGYI VHGIKRRSSS FNTQRIEHIY QERHDPEARF 70 80 90 100 110 120 FLHYGDMTDS TNLLRIVQQT QPHEIYNLAA QSHVQVSFET PEYTANADAI GTLRMLEAIR 130 140 150 160 170 180 ILGLIHRTRF YQASTSELYG LAQEIPQNEK TPFYPRSPYA AAKLYAYWIV VNYREAYGMH 190 200 210 220 230 240 ASNGILFNHE SPLRGETFVT RKITRAAAAI SLGKQEVLYL GNLDAQRDWG HAREYVRGMW 250 260 270 280 290 300 MMCQQDRPGD YVLATGVTTS VRTFVEWAFE ETGMTIEWVG EGIEERGIDA ATGKCVVAVD 310 320 330 340 350 PRYFRPTEVD LLLGDATKAR QVLGWRHETS VRDLACEMVR EDLSYLRGTR Q

References

[1]

"Mutation in GDP-fucose synthesis genes of Sinorhizobium fredii alters Nod factors and significantly decreases competitiveness to nodulate soybeans." Lamrabet Y., Bellogin R.A., Cubo T., Espuny R., Gil A., Krishnan H.B., Megias M., Ollero F.J., Pueppke S.G., Ruiz-Sainz J.E., Spaink H.P., Tejero-Mateo P., Thomas-Oates J., Vinardell J.M. Mol. Plant Microbe Interact. 12:207-217(1999) [PubMed: 10065558] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: HH103.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF072888 Genomic DNA. Translation: AAC27750.1.
3D structure databases
SMR	O85713. Positions 4-347.
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.2.1.47. 2200.
Family and domain databases
InterPro	IPR001509. Epimerase_deHydtase. IPR006368. GDP_Man_deHydtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR10366:SF32. GDP_mann_dehyd. 1 hit.
Pfam	PF01370. Epimerase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01472. gmd. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NOEL_RHIFR

Accession

Primary (citable) accession number: O85713

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1998
Last modified:	February 9, 2010
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)