GDP-mannose 4,6 dehydratase 1 - Caenorhabditis elegans

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Q18801 (GMD1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
GDP-mannose 4,6 dehydratase 1
EC=4.2.1.47

Alternative name(s):
Bacillus thuringiensis toxin-resistant protein 1
Short name=Bt toxin-resistant protein 1
GDP-D-mannose dehydratase
Short name=GMD

Gene names

Name:	bre-1
Synonyms:	gmd-1
ORF Names:	C53B4.7

Organism

Caenorhabditis elegans

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	399 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Conversion of GDP-D-mannose to GDP-4-keto-6-D-deoxymannose. Involved in susceptibility to pore-forming crystal toxins in conjunction with bre-2, bre-3, bre-4, and bre-5. Has a role in determining brood size. Ref.1 Ref.3 Ref.4 Ref.5
Catalytic activity	GDP-mannose = GDP-4-dehydro-6-deoxy-D-mannose + H₂O. Ref.1
Cofactor	NADP By similarity.
Pathway	Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 1/2.
Developmental stage	Expressed throughout development, showing up-regulation between stages L2 and L4. Ref.1
Disruption phenotype	Worms exhibit resistance to the Cry5B toxin produced by Bacillus thuringiensis. This is thought to be due to mutants having reduced population of glycolipids which are targeted by the Cry5B protein. Mutants also have reduced brood sizes at only 12% of wild-type N2. Ref.3
Sequence similarities	Belongs to the GDP-mannose 4,6-dehydratase family.
Biophysicochemical properties	Temperature dependence: Optimum temperature is 30 degrees Celsius. Ref.1

Ontologies

Keywords
Biological process	Insecticide resistance
Coding sequence diversity	Alternative splicing
Ligand	NADP
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	GDP-L-fucose biosynthetic process Inferred from direct assay Ref.1. Source: WormBase GDP-mannose metabolic process Inferred from direct assay Ref.1. Source: WormBase formation of infection structure on or near host Inferred from mutant phenotype Ref.3. Source: UniProtKB response to insecticide Inferred from mutant phenotype Ref.3. Source: UniProtKB striated muscle myosin thick filament assembly Inferred from mutant phenotype. Source: WormBase
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	GDP-mannose 4,6-dehydratase activity Inferred from direct assay Ref.1. Source: UniProtKB coenzyme binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform b (identifier: Q18801-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform a (identifier: Q18801-2) The sequence of this isoform differs from the canonical sequence as follows: 1-23: MPTGKSESSDISEVVGNMEISKV → MADQNAKI

Isoform c (identifier: Q18801-3) The sequence of this isoform differs from the canonical sequence as follows: 1-31: Missing.
Note: No experimental confirmation available.

Isoform d (identifier: Q18801-4) The sequence of this isoform differs from the canonical sequence as follows: 1-24: MPTGKSESSDISEVVGNMEISKVE → MDSSAEQ
Note: No experimental confirmation available.

Isoform e (identifier: Q18801-5) The sequence of this isoform differs from the canonical sequence as follows: 1-24: MPTGKSESSDISEVVGNMEISKVE → MNSHDSKIFCQTCSNGNNQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 399

399

GDP-mannose 4,6 dehydratase 1

PRO_0000201708

Sites

Active site

183

By similarity

Active site

185

Nucleophile By similarity

Active site

207

Nucleophile By similarity

Binding site

211

NADP By similarity

Natural variations

Alternative sequence

1 – 31

Missing in isoform c.

VSP_032084

Alternative sequence

1 – 24

MPTGK…ISKVE → MDSSAEQ in isoform d.

VSP_032086

Alternative sequence

1 – 24

MPTGK…ISKVE → MNSHDSKIFCQTCSNGNNQ in isoform e.

VSP_032085

Alternative sequence

1 – 23

MPTGK…EISKV → MADQNAKI in isoform a.

VSP_013810

Experimental info

Mutagenesis

232

G → E in ye4; resistant to Bacillus thuringiensis crystal5B toxin and reduced brood size. Ref.4

Sequences

Sequence		Length	Mass (Da)
Isoform b [UniParc]. Last modified May 24, 2005. Version 3. Checksum: 51E3A872ACF0983A Show »	FASTA	399	44,489
10 20 30 40 50 60 MPTGKSESSD ISEVVGNMEI SKVEGLEACI GMSHEVSTTP AAELAAFRAR KVALITGISG 70 80 90 100 110 120 QDGSYLAELL LSKGYKVHGI IRRSSSFNTA RIEHLYSNPI THHGDSSFSL HYGDMTDSSC 130 140 150 160 170 180 LIKLISTIEP TEVYHLAAQS HVKVSFDLPE YTAEVDAVGT LRLLDAIHAC RLTEKVRFYQ 190 200 210 220 230 240 ASTSELYGKV QEIPQSEKTP FYPRSPYAVA KMYGYWIVVN YREAYNMFAC NGILFNHESP 250 260 270 280 290 300 RRGETFVTRK ITRSVAKISL GQQESIELGN LSALRDWGHA REYVEAMWRI LQHDSPDDFV 310 320 330 340 350 360 IATGKQFSVR EFCNLAFAEI GEVLQWEGEG VEEVGKNKDG VIRVKVSPKY YRPTEVETLL 370 380 390 GNAEKAKKTL GWEAKVTVPE LVKEMVASDI ILMKSNPMA « Hide
Isoform a [UniParc]. Checksum: B3F65EA219902594 Show »	FASTA	384	42,954
10 20 30 40 50 60 MADQNAKIEG LEACIGMSHE VSTTPAAELA AFRARKVALI TGISGQDGSY LAELLLSKGY 70 80 90 100 110 120 KVHGIIRRSS SFNTARIEHL YSNPITHHGD SSFSLHYGDM TDSSCLIKLI STIEPTEVYH 130 140 150 160 170 180 LAAQSHVKVS FDLPEYTAEV DAVGTLRLLD AIHACRLTEK VRFYQASTSE LYGKVQEIPQ 190 200 210 220 230 240 SEKTPFYPRS PYAVAKMYGY WIVVNYREAY NMFACNGILF NHESPRRGET FVTRKITRSV 250 260 270 280 290 300 AKISLGQQES IELGNLSALR DWGHAREYVE AMWRILQHDS PDDFVIATGK QFSVREFCNL 310 320 330 340 350 360 AFAEIGEVLQ WEGEGVEEVG KNKDGVIRVK VSPKYYRPTE VETLLGNAEK AKKTLGWEAK 370 380 VTVPELVKEM VASDIILMKS NPMA « Hide
Isoform c [UniParc]. Checksum: 9B6E737154AAE70C Show »	FASTA	368	41,309
10 20 30 40 50 60 MSHEVSTTPA AELAAFRARK VALITGISGQ DGSYLAELLL SKGYKVHGII RRSSSFNTAR 70 80 90 100 110 120 IEHLYSNPIT HHGDSSFSLH YGDMTDSSCL IKLISTIEPT EVYHLAAQSH VKVSFDLPEY 130 140 150 160 170 180 TAEVDAVGTL RLLDAIHACR LTEKVRFYQA STSELYGKVQ EIPQSEKTPF YPRSPYAVAK 190 200 210 220 230 240 MYGYWIVVNY REAYNMFACN GILFNHESPR RGETFVTRKI TRSVAKISLG QQESIELGNL 250 260 270 280 290 300 SALRDWGHAR EYVEAMWRIL QHDSPDDFVI ATGKQFSVRE FCNLAFAEIG EVLQWEGEGV 310 320 330 340 350 360 EEVGKNKDGV IRVKVSPKYY RPTEVETLLG NAEKAKKTLG WEAKVTVPEL VKEMVASDII LMKSNPMA « Hide
Isoform d [UniParc]. Checksum: 7B23BF509E6CE43D Show »	FASTA	382	42,702
10 20 30 40 50 60 MDSSAEQGLE ACIGMSHEVS TTPAAELAAF RARKVALITG ISGQDGSYLA ELLLSKGYKV 70 80 90 100 110 120 HGIIRRSSSF NTARIEHLYS NPITHHGDSS FSLHYGDMTD SSCLIKLIST IEPTEVYHLA 130 140 150 160 170 180 AQSHVKVSFD LPEYTAEVDA VGTLRLLDAI HACRLTEKVR FYQASTSELY GKVQEIPQSE 190 200 210 220 230 240 KTPFYPRSPY AVAKMYGYWI VVNYREAYNM FACNGILFNH ESPRRGETFV TRKITRSVAK 250 260 270 280 290 300 ISLGQQESIE LGNLSALRDW GHAREYVEAM WRILQHDSPD DFVIATGKQF SVREFCNLAF 310 320 330 340 350 360 AEIGEVLQWE GEGVEEVGKN KDGVIRVKVS PKYYRPTEVE TLLGNAEKAK KTLGWEAKVT 370 380 VPELVKEMVA SDIILMKSNP MA « Hide
Isoform e [UniParc]. Checksum: DA5674C9420E58FD Show »	FASTA	394	44,063
10 20 30 40 50 60 MNSHDSKIFC QTCSNGNNQG LEACIGMSHE VSTTPAAELA AFRARKVALI TGISGQDGSY 70 80 90 100 110 120 LAELLLSKGY KVHGIIRRSS SFNTARIEHL YSNPITHHGD SSFSLHYGDM TDSSCLIKLI 130 140 150 160 170 180 STIEPTEVYH LAAQSHVKVS FDLPEYTAEV DAVGTLRLLD AIHACRLTEK VRFYQASTSE 190 200 210 220 230 240 LYGKVQEIPQ SEKTPFYPRS PYAVAKMYGY WIVVNYREAY NMFACNGILF NHESPRRGET 250 260 270 280 290 300 FVTRKITRSV AKISLGQQES IELGNLSALR DWGHAREYVE AMWRILQHDS PDDFVIATGK 310 320 330 340 350 360 QFSVREFCNL AFAEIGEVLQ WEGEGVEEVG KNKDGVIRVK VSPKYYRPTE VETLLGNAEK 370 380 390 AKKTLGWEAK VTVPELVKEM VASDIILMKS NPMA « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Reconstitution in vitro of the GDP-fucose biosynthetic pathways of Caenorhabditis elegans and Drosophila melanogaster." Rhomberg S., Fuchsluger C., Rendic D., Paschinger K., Jantsch V., Kosma P., Wilson I.B.H. FEBS J. 273:2244-2256(2006) [PubMed: 16650000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, ALTERNATIVE SPLICING.
[2]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.
[3]	"Bacillus thuringiensis (Bt) toxin susceptibility and isolation of resistance mutants in the nematode Caenorhabditis elegans." Marroquin L.D., Elyassnia D., Griffitts J.S., Feitelson J.S., Aroian R.V. Genetics 155:1693-1699(2000) [PubMed: 10924467] [Abstract] Cited for: IDENTIFICATION, FUNCTION, DISRUPTION PHENOTYPE.
[4]	"Resistance to Bacillus thuringiensis toxin in Caenorhabditis elegans from loss of fucose." Barrows B.D., Haslam S.M., Bischof L.J., Morris H.R., Dell A., Aroian R.V. J. Biol. Chem. 282:3302-3311(2007) [PubMed: 17135259] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-232.
[5]	"Resistance is non-futile: resistance to Cry5B in the nematode Caenorhabditis elegans." Barrows B.D., Griffitts J.S., Aroian R.V. J. Invertebr. Pathol. 95:198-200(2007) [PubMed: 17482642] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM231683 mRNA. Translation: CAJ77752.1. AM231684 mRNA. Translation: CAJ77753.1. Z68215 Genomic DNA. Translation: CAA92455.2. Z68215 Genomic DNA. Translation: CAC42269.1. Z68215 Genomic DNA. Translation: CAC42270.1. Z68215 Genomic DNA. Translation: CAL49435.1. Z68215 Genomic DNA. Translation: CAL49436.1.
PIR	T20182.
RefSeq	NP_001076668.1. NM_001083199.1. NP_001076669.1. NM_001083200.1. NP_001076670.1. NM_001083201.1. NP_501563.1. NM_069162.5. NP_501564.1. NM_069163.2.
UniGene	Cel.13248.
3D structure databases
ProteinModelPortal	Q18801.
SMR	Q18801. Positions 50-396.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q18801. 1 interaction.
STRING	Q18801.
Proteomic databases
PRIDE	Q18801.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	C53B4.7b; C53B4.7b; C53B4.7.
GeneID	177717.
KEGG	cel:C53B4.7.
UCSC	C53B4.7a.1. c. elegans.
Organism-specific databases
CTD	177717.
WormBase	C53B4.7a; CE27116; WBGene00000266; bre-1. C53B4.7b; CE27117; WBGene00000266; bre-1. C53B4.7c; CE23608; WBGene00000266; bre-1. C53B4.7d; CE40447; WBGene00000266; bre-1. C53B4.7e; CE40448; WBGene00000266; bre-1.
Phylogenomic databases
eggNOG	meNOG06965.
GeneTree	EMGT00050000011127.
InParanoid	Q18801.
OMA	VKFYQAG.
PhylomeDB	Q18801.
Gene expression databases
ArrayExpress	Q18801.
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.
KO	K01711.
PANTHER	PTHR10366:SF32. GDP_mann_dehyd. 1 hit.
Pfam	PF01370. Epimerase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01472. Gmd. 1 hit.
ProtoNet	Search...
Other
NextBio	898062.

Entry information

Entry name

GMD1_CAEEL

Accession

Primary (citable) accession number: Q18801
Secondary accession number(s): Q067Y3

Q8T8N3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 24, 2005
Last modified:	December 14, 2011
This is version 88 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Sites

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents