Q2U5P7 (RGLC_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable rhamnogalacturonate lyase C
EC=4.2.2.-

Gene names

Name:	rglC
ORF Names:	AO090113000057

Organism

Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]

Taxonomic identifier

510516 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	695 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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 By similarity.
Catalytic activity	Cleaves the alpha-1,4 linkage of RG-I backbone between a rhamnose and a galacturonate, thereby creating an unsaturated bond between carbons 4 and 5 of the galacturonate residue.
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	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro lyase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 695	674	Probable rhamnogalacturonate lyase C		PRO_0000394380
Amino acid modifications
	Glycosylation	28	1	N-linked (GlcNAc...) Potential
	Glycosylation	96	1	N-linked (GlcNAc...) Potential
	Glycosylation	118	1	N-linked (GlcNAc...) Potential
	Glycosylation	144	1	N-linked (GlcNAc...) Potential
	Glycosylation	199	1	N-linked (GlcNAc...) Potential
	Glycosylation	285	1	N-linked (GlcNAc...) Potential
	Glycosylation	532	1	N-linked (GlcNAc...) Potential
	Glycosylation	638	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q2U5P7 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: E6032805EBE4EE1A	FASTA	695	77,249
	10 20 30 40 50 60 MFLPSRKALA FLACLASHSV ALLTTSENST HFNLANDRFS IALAKSNGHI VDVQLDGQDL 70 80 90 100 110 120 LGPVDGNAGK GPYLDCSCIP SGFWTPGSGA HLELINGTDS TGTAYGGLYM SATYAGTNQT 130 140 150 160 170 180 LSQWFFLRGE ETGLHAFSRV TYFNETTPSL RSLGELRTLF RPSTDLWTHF STSDGNYGPK 190 200 210 220 230 240 PLGSNSGLVV QDATTYIGNV TDDPYVSQYS DYFTKYTLAE SWRNHDVHGL FSDGSSSSDG 250 260 270 280 290 300 STFGAWLVHN TVETYYGGPL HSDLVVDGIV YNYLVSGHHG APTPNLTHGF DRTWGPQFYY 310 320 330 340 350 360 FNRGDSETTL ADLRADAAKY ADPEWNAEFY DSIADHIPNF TPSTGRTTFK GKVSLPKGAK 370 380 390 400 410 420 RPIIVLSEDG QDFQLNVFNT ESLQYWAEID KSGSFSIPRV VEGTYRITIY ADEIFGWFIQ 430 440 450 460 470 480 DHVKVLKSQS KDYSFTWKEE SAGKEIWRIG IPDKSSGEYL HGYAPDTSKP LQPEQHRIYW 490 500 510 520 530 540 GKYDYPADFP EGINFHVGKS DPSQDLNYIH WAFFPSQGNH LRTEPYYDNV NNWTVTFDLT 550 560 570 580 590 600 ADQLHNTNTA TFTVQIAGAK TANGNAKWTP VEGKYSNLPW TVNVNGRYES TWVIPYWRSG 610 620 630 640 650 660 SCGVRSAVSC QNIEQKFAFP SKNLQEGKNE FVLSLPFNAS STETALLPDA LYVQARVMGS 670 680 690 RLDPARPAPN PLVNSNLGFG RDNPIMEFSN NRIIT

References

[1]

"Genome sequencing and analysis of Aspergillus oryzae." Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H. Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 42149 / RIB 40.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP007166 Genomic DNA. Translation: BAE63118.1.
3D structure databases
ProteinModelPortal	Q2U5P7.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAORAT00011669; CADAORAP00011433; CADAORAG00011669.
Phylogenomic databases
eggNOG	NOG43733.
HOGENOM	HOG000217023.
OrthoDB	EOG4MPMZC.
Family and domain databases
Gene3D	2.60.120.260. 1 hit. 2.60.40.1120. 1 hit.
InterPro	IPR013784. Carb-bd-like_fold. IPR014766. CarboxyPept_regulatory_dom. IPR011013. Gal_mutarotase_SF_dom. IPR008979. Galactose-bd-like. [Graphical view]
SUPFAM	SSF49452. CBD_4. 1 hit. SSF49785. Gal_bind_like. 1 hit. SSF74650. Gal_mut_like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

RGLC_ASPOR

Accession

Primary (citable) accession number: Q2U5P7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 18, 2010
Last sequence update:	January 24, 2006
Last modified:	May 29, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program