Reviewed, UniProtKB/Swiss-Prot Q9STI6 (GAE5_ARATH)

Names and origin

Protein names

Recommended name:
    UDP-glucuronate 4-epimerase 5
    EC=5.1.3.6
Alternative name(s):
    UDP-glucuronic acid epimerase 5

Gene names

Name:	GAE5
Ordered Locus Names:	At4g12250
ORF Names:	T4C9.90

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	436 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components.
Catalytic activity	UDP-glucuronate = UDP-D-galacturonate.
Subunit structure	Homodimer By similarity.
Subcellular location	Golgi apparatus › Golgi stack membrane; Multi-pass membrane protein Potential.
Tissue specificity	In leaves, pollen and siliques, but not in roots or flowers. Ref.4 Ref.5
Sequence similarities	Belongs to the sugar epimerase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Golgi apparatus Membrane
Domain	Transmembrane
Ligand	NAD
Molecular function	Isomerase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW cellular metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-glucuronate 4-epimerase 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 – 436	436	UDP-glucuronate 4-epimerase 5		PRO_0000292600
Regions
	Transmembrane	36 – 56	21	Potential
	Transmembrane	95 – 115	21	Potential
	Nucleotide binding	97 – 128	32	NAD By similarity
	Compositional bias	221 – 224	4	Poly-Ser
Sites
	Active site	247	1	Proton acceptor By similarity
Experimental info
	Sequence conflict	116	1	R → Q in AAK93670. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9STI6-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 2D9B645D80735C14	FASTA	436	48,165
	10 20 30 40 50 60 MSHLDDLPST PGKYKTDKVP PYGILHHHRY LRLSKLTLWA SLFLALFLFY LVLSPPPSPS 70 80 90 100 110 120 RRNLNDSSSI SAAKYGGSHW EKQVRKSARP RSHGGLTVLV TGASGFVGTH VSIALRRRGD 130 140 150 160 170 180 GVLGLDNFNR YYDPKLKRAR QGLLERSGVF VVEGDINDAV LLRKLFDVVL FTHVMHLAAQ 190 200 210 220 230 240 AGVRYAMQNP GSYVNSNIAG FVNLLEVSKS ANPQPAIVWA SSSSVYGLNS KVPFSEKDRT 250 260 270 280 290 300 DQPASLYAAT KKAGEGIAHT YNHIYGLSLT GLRFFTVYGP WGRPDMAYFF FTKDILKGKT 310 320 330 340 350 360 ITVFESPDKG SVARDFTYID DIVKGCLGAL DTAEKSTGSG GKKKGPAMFR IYNLGNTSPV 370 380 390 400 410 420 PVTKLVTILE KLLKMKAKKK IMPLPRNGDV EFTHANITLA QAELGYKPAV DLETGLKKFV 430 KWYMGFYTGS KKKSSW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"Molecular genetics of nucleotide sugar interconversion pathways in plants." Reiter W.-D., Vanzin G.F. Plant Mol. Biol. 47:95-113(2001) [PubMed: 11554483] [Abstract] Cited for: IDENTIFICATION, NOMENCLATURE.
[4]	"The biosynthesis of D-galacturonate in plants. Functional cloning and characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from Arabidopsis." Moelhoej M., Verma R., Reiter W.-D. Plant Physiol. 135:1221-1230(2004) [PubMed: 15247385] [Abstract] Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
[5]	"Identification and characterization of a UDP-D-glucuronate 4-epimerase in Arabidopsis." Usadel B., Schlueter U., Moelhoej M., Gipmans M., Verma R., Kossmann J., Reiter W.-D., Pauly M. FEBS Lett. 569:327-331(2004) [PubMed: 15225656] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL080318 Genomic DNA. Translation: CAB45972.1. AL161533 Genomic DNA. Translation: CAB78268.1. AY050993 mRNA. Translation: AAK93670.1. AY150403 mRNA. Translation: AAN12948.1.
IPI	IPI00529597.
PIR	T48135.
RefSeq	NP_192962.1.
UniGene	At.48849
3D structure databases
HSSP	HSSP built from PDB template 1EK6 based on UniProtKB Q14376.
ModBase	Search...
Genome annotation databases
GeneID	826833.
GenomeReviews	Gene locus AT4G12250 in contig CT486007_GR.
KEGG	ath:AT4G12250.
NMPDR	fig|3702.1.peg.18900.
Organism-specific databases
TAIR	At4g12250.
Phylogenomic databases
OMA	EFTHANI.
Enzyme and pathway databases
BRENDA	5.1.3.6. 302.
Gene expression databases
Genevestigator	Q9STI6.
Family and domain databases
InterPro	IPR001509. Epimerase_deHydtase. IPR016040. NAD(P)-bd_dom. IPR008089. Nuc_sugar_epim. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF01370. Epimerase. 1 hit. [Graphical view]
PRINTS	PR01713. NUCEPIMERASE.
ProtoNet	Search...

Entry information

Entry name

GAE5_ARATH

Accession

Primary (citable) accession number: Q9STI6
Secondary accession number(s): Q949N3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)