Q5BCI8 (MANBA_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable beta-mannosidase A
EC=3.2.1.25

Alternative name(s):
Mannanase A
Short name=Mannase A

Gene names

Name:	mndA
ORF Names:	AN1742

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	940 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	Exoglycosidase that cleaves the single beta-linked mannose residue from the non-reducing end of all N-linked glycoprotein oligosaccharides. Involved in the degradation of mannan and galactomannan By similarity.
Catalytic activity	Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.
Pathway	Glycan metabolism; N-glycan degradation.
Subunit structure	Homodimer By similarity.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 2 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	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-mannosidase activity Inferred from electronic annotation. Source: EC
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 – 940	919	Probable beta-mannosidase A		PRO_0000394649
Sites
	Active site	476	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	15	1	N-linked (GlcNAc...) Potential
	Glycosylation	39	1	N-linked (GlcNAc...) Potential
	Glycosylation	79	1	N-linked (GlcNAc...) Potential
	Glycosylation	245	1	N-linked (GlcNAc...) Potential
	Glycosylation	314	1	N-linked (GlcNAc...) Potential
	Glycosylation	321	1	N-linked (GlcNAc...) Potential
	Glycosylation	344	1	N-linked (GlcNAc...) Potential
	Glycosylation	534	1	N-linked (GlcNAc...) Potential
	Glycosylation	605	1	N-linked (GlcNAc...) Potential
	Glycosylation	626	1	N-linked (GlcNAc...) Potential
	Glycosylation	653	1	N-linked (GlcNAc...) Potential
	Glycosylation	733	1	N-linked (GlcNAc...) Potential
	Glycosylation	761	1	N-linked (GlcNAc...) Potential
	Glycosylation	785	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5BCI8 [UniParc]. Last modified April 26, 2005. Version 1. Checksum: 45E1CBB33D2AFAF0	FASTA	940	105,765
	10 20 30 40 50 60 MHFHGIATQA VLASNITTGS GRHVSLSDVK WTLSSSALNS TVPASLPSQA HLDLLNAGVI 70 80 90 100 110 120 DDPYYGLNEI DLQWIAQANW TYTSDPIPDL LEEYESTWLV FEGLDTFATV TFCGHNIAST 130 140 150 160 170 180 NNQFRQYAFD VSSALKECTG GPVVRIDFAS APNTVDAIAA DPKTPVWPVQ LTAQLPNRWL 190 200 210 220 230 240 MRKQQSDFGW DWGPAFAPCG PWKPAYVVQL EKTAPIHVLN TDLDIYRQGN INHLPPDQKQ 250 260 270 280 290 300 PWVVNASIDF IGRLPAEPRL LIEIKELETG DVLASQISDS VTLIGTSITG VTTLKDASPK 310 320 330 340 350 360 LWWPSSLGAQ NLYNVTITVF NKTEEVARIT KRTGFRTIFL NQRNITATQL SQGIAPGANW 370 380 390 400 410 420 HFEVNGKEFY AKGSNFIPPD TFWPRVTKQK MTRLLDAVVA GNQNMLRIWS SGAYLPDFIY 430 440 450 460 470 480 DLADERGILL WSEFQFSDSM YPVDEDFLDN VAQEVVYNVR RVNHHPSLAL WAGGNEIESL 490 500 510 520 530 540 MLPLTREADP DNYPKYLAEY EKLYISLILP LVYENTRSIS YSPSSTTEGY LSVNLSAPVP 550 560 570 580 590 600 MTERYENDEP GAYYGDTDYY NYDTTVSFDY SIYPVGRFAN EFGFHSMPSL QTWQQVADPE 610 620 630 640 650 660 DLYFNSTTVV IHNRHYTSEG YGRIENSSRG MAEMTLGVER YYPIPDNPDS VANFSAWCLA 670 680 690 700 710 720 TQLFQADFYK SQIQFYRRGS GMPERQLGSL YWQLEDIWQG PTWAGIEYDG RWKVLHYVAR 730 740 750 760 770 780 DVYQPIIVSP FWNYTTGDLE IYVTADLWES AAGTVNLKWL NLSGEQIIDN AGTPTEIPFT 790 800 810 820 830 840 VGAINTTKVY STNIHDLNLP DTRASILTLS LSSQANLPNA AVKTSLTHEN HFTPSFPKDL 850 860 870 880 890 900 ELVNPGLELS YDAHSGIFTV EAKSGVSLYT WLDYPAGLVG YFTENAFLLV PGQKKKVQFV 910 920 930 940 VQDGPKDQDW EWQSEVTVRS LWDQKSSTFL YALRVATGRP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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	AACD01000027 Genomic DNA. Translation: EAA64028.1. BN001307 Genomic DNA. Translation: CBF85479.1.
RefSeq	XP_659346.1. XM_654254.1.
3D structure databases
ProteinModelPortal	Q5BCI8.
ModBase	Search...
Protein family/group databases
CAZy	GH2. Glycoside Hydrolase Family 2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00008389; CADANIAP00008389; CADANIAG00008389.
GeneID	2874889.
KEGG	ani:AN1742.2.
Phylogenomic databases
eggNOG	COG3250.
HOGENOM	HOG000216059.
KO	K01192.
OMA	WAGGNEI.
OrthoDB	EOG47DDQ6.
Enzyme and pathway databases
UniPathway	UPA00280.
Family and domain databases
Gene3D	2.60.40.320. 1 hit. 3.20.20.80. 2 hits.
InterPro	IPR008979. Galactose-bd-like. IPR013812. Glyco_hydro_2/20_Ig-like. IPR006102. Glyco_hydro_2_Ig-like. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00703. Glyco_hydro_2. 1 hit. [Graphical view]
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF49303. Glyco_hydro_2Ig. 2 hits. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00719. GLYCOSYL_HYDROL_F2_1. False negative. PS00608. GLYCOSYL_HYDROL_F2_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANBA_EMENI

Accession

Primary (citable) accession number: Q5BCI8
Secondary accession number(s): C8VP45

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 15, 2010
Last sequence update:	April 26, 2005
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program