Q5AX45 (RGLA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rhamnogalacturonate lyase A
EC=4.2.2.23

Gene names

Name:	rglA
ORF Names:	AN7135

Organism

Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) [Reference proteome]

Taxonomic identifier

227321 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella › Emericella nidulans › mitosporic Emericella nidulans

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Degrades the rhamnogalacturonan I (RG-I) backbone of pectin. Active against linseed rhamnogalacturonan. Ref.1
Catalytic activity	Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the polysaccharide lyase 4 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cell wall biogenesis/degradation Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Lyase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pectin catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro carbon-oxygen lyase activity, acting on polysaccharides Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 527	507	Rhamnogalacturonate lyase A		PRO_0000394371
Amino acid modifications
	Glycosylation	27	1	N-linked (GlcNAc...) Potential
	Glycosylation	46	1	N-linked (GlcNAc...) Potential
	Glycosylation	351	1	N-linked (GlcNAc...) Potential
	Disulfide bond	50 ↔ 93		By similarity
	Disulfide bond	184 ↔ 193		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5AX45 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: D07A2C92955DB47D	FASTA	527	56,381
	10 20 30 40 50 60 MLSKTFLLSS AVLWARVANA AFGITDNGSS YTIDANSPNP LKFTVNKSSC DITSIVYYGS 70 80 90 100 110 120 EFQYSGKGSH IGSGLGSATV SATQSGDYIK VTCDTSSLTH YFVVHNGDPI IHMATYITAE 130 140 150 160 170 180 PDIGELRFIA RLNSNLLPNE EPFGDVSTTS GGSAIEGSDV FLVNGETRSK FYSSERFIDD 190 200 210 220 230 240 HRHCISGSAH RVCMILNQYE SSSGGPFFRD INSNNGGDYN ALYWYMNSGH VQTESFRTGL 250 260 270 280 290 300 HGPYSMYFSR SGTPSTNIDT SFFASLGIKG YVAANGRGTV TGKASGADSS MDWVVHWYNN 310 320 330 340 350 360 DAQYWTYTAS DGSFTSPAMK PGTYTMKYYQ GEFPVAETTV TVSAGSSTTK NISGSVKTGT 370 380 390 400 410 420 TIFKIGEWDG QPTGFRNADK QLRMHPSDSR MDSWSSTYTV GSSSLSDFPM AVFKSVNNPV 430 440 450 460 470 480 TIKFTATSAQ TGAATLRIGT TLSFAGGRPQ ATINSYTGPA PSAPTNLNSR GVTRGAYRGL 490 500 510 520 GEVYDVSVPA GTIVTGENTI TISVISGSSG DAFLSPNVVF DCIELFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls." Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R. Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
[3]	"The 2008 update of the Aspergillus nidulans genome annotation: a community effort." Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G. , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G. Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ490504 mRNA. Translation: ABF50880.1. AACD01000122 Genomic DNA. Translation: EAA61387.1. BN001304 Genomic DNA. Translation: CBF79004.1.
RefSeq	XP_664739.1. XM_659647.1.
3D structure databases
ProteinModelPortal	Q5AX45.
SMR	Q5AX45. Positions 21-527.
ModBase	Search...
Protein family/group databases
mycoCLAP	RGL4A_EMENI.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00000323; CADANIAP00000323; CADANIAG00000323.
GeneID	2870208.
KEGG	ani:AN7135.2.
Phylogenomic databases
eggNOG	NOG73253.
HOGENOM	HOG000171008.
OMA	RSKFYSS.
OrthoDB	EOG4F7RT8.
Family and domain databases
Gene3D	2.60.120.260. 1 hit. 2.60.40.1120. 1 hit. 2.70.98.10. 1 hit.
InterPro	IPR013784. Carb-bd-like_fold. IPR014766. CarboxyPept_regulatory_dom. IPR011013. Gal_mutarotase_SF_dom. IPR008979. Galactose-bd-like. IPR014718. Glyco_hydro-type_carb-bd_sub. IPR016590. Rhamnogalacturonase_B. IPR015364. RhgB_N. [Graphical view]
Pfam	PF09284. RhgB_N. 1 hit. [Graphical view]
PIRSF	PIRSF011794. Rhamnogalacturonase_B. 1 hit.
SUPFAM	SSF49452. CBD_4. 1 hit. SSF49785. Gal_bind_like. 1 hit. SSF74650. Gal_mut_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RGLA_EMENI

Accession

Primary (citable) accession number: Q5AX45
Secondary accession number(s): C8VD91, Q1HFS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	April 26, 2005
Last modified:	May 29, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program