Q5BDV3 (ABFC_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-N-arabinofuranosidase C
Short name=ABF C
Short name=Arabinosidase C
EC=3.2.1.55

Gene names

Name:	abfC
ORF Names:	AN1277

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	504 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	Alpha-N-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides. Ref.1
Catalytic activity	Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.
Pathway	Glycan metabolism; L-arabinan degradation.
Subcellular location	Secreted Probable.
Sequence similarities	Belongs to the glycosyl hydrolase 51 family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-arabinose metabolic process Inferred from electronic annotation. Source: InterPro arabinan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway arabinose metabolic process Inferred from direct assay Ref.1. Source: UniProtKB pectin catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alpha-N-arabinofuranosidase activity 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 – ?		Potential
	Chain	? – 504		Alpha-N-arabinofuranosidase C		PRO_0000394616
Amino acid modifications
	Glycosylation	81	1	N-linked (GlcNAc...) Potential
	Glycosylation	152	1	N-linked (GlcNAc...) Potential
	Glycosylation	269	1	N-linked (GlcNAc...) Potential
	Glycosylation	329	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5BDV3 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 0E79FD944F10970D	FASTA	504	56,554
	10 20 30 40 50 60 MTTFTKLSEQ EAPGISIHPD RRISKINPNI YAGFAEHMGR CIYGGIYDPG NPLSDENGFR 70 80 90 100 110 120 KDVLEALKEL KVPVIRYPGG NFTATYHWID GVGPRDQRPA RPELAWLGTE TNQFGTDEFL 130 140 150 160 170 180 KWCEVLGTEP YLCLNMGTGT LDEALAWVDY CNGTRDTYYA NLRRKNGREE PYNVKYWALG 190 200 210 220 230 240 NEVWGPWQVE QSTKEEYAHK AYQWAKALKL LDPSIELILC GKEGPTSWDY YTLKQTMLPV 250 260 270 280 290 300 HSPLSTSAVP LIDMHSIHLY TAHSSHLPNV TAPLAAERAI EITSSLIDLA RVENGVPPEQ 310 320 330 340 350 360 RRPTICFDEW NVWDPIRAEG SKGAEESYNL SDALAVGVWL NVFVRKSKDV GMACIAQSVN 370 380 390 400 410 420 VISPLMTTKD GIVKQTTWWP LYLFSNYMRG WTISAHISVS AYEGETHPKW VRGVKDTPWL 430 440 450 460 470 480 DVSATLGEDG YVNVVVINIH EEKGIEAKLD GPSGEVTVFT VTGDNPAVTN MKGKEEVGLV 490 500 ETKWDAQGPY VFPKHSLTLL RWKA

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	DQ490471 mRNA. Translation: ABF50847.1. AACD01000017 Genomic DNA. Translation: EAA65870.1. BN001308 Genomic DNA. Translation: CBF87808.1.
RefSeq	XP_658881.1. XM_653789.1.
3D structure databases
ProteinModelPortal	Q5BDV3.
ModBase	Search...
Protein family/group databases
CAZy	GH51. Glycoside Hydrolase Family 51.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00001344; CADANIAP00001344; CADANIAG00001344.
GeneID	2877053.
KEGG	ani:AN1277.2.
Phylogenomic databases
eggNOG	COG3534.
HOGENOM	HOG000236895.
KO	K01209.
OMA	DEWNVWD.
OrthoDB	EOG45F0XW.
Enzyme and pathway databases
UniPathway	UPA00667.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR010720. Alpha-L-AF_C. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF06964. Alpha-L-AF_C. 1 hit. [Graphical view]
SMART	SM00813. Alpha-L-AF_C. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ABFC_EMENI

Accession

Primary (citable) accession number: Q5BDV3
Secondary accession number(s): C8VSG2, Q1HFV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	April 26, 2005
Last modified:	May 1, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program