Q5B833 (MANB_EMENI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mannan endo-1,4-beta-mannosidase B
EC=3.2.1.78

Alternative name(s):
Endo-beta-1,4-mannanase B

Gene names

Name:	manB
ORF Names:	AN3297

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	387 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	Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and gum guar. Ref.1
Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Subcellular location	Secreted By similarity.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Sequence caution	The sequence CBF83007.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA63265.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mannan catabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mannan endo-1,4-beta-mannosidase 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 – 24	24	Potential
	Chain	25 – 387	363	Mannan endo-1,4-beta-mannosidase B		PRO_0000393708
Sites
	Active site	204	1	Proton donor By similarity
	Active site	312	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	107	1	N-linked (GlcNAc...) Potential
	Glycosylation	165	1	N-linked (GlcNAc...) Potential
	Glycosylation	286	1	N-linked (GlcNAc...) Potential
	Glycosylation	318	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5B833 [UniParc]. Last modified April 20, 2010. Version 2. Checksum: 8CC8A4C1253E7823	FASTA	387	43,725
	10 20 30 40 50 60 MRLIHAVLGL LAGAAPALVA ASPAAPIGNG RDQVSKAVGR HFEIDGKVQY FAGTNCWWLG 70 80 90 100 110 120 NLLNDFEVEL AVSQIAETGY KVVRTWGFFG VNDPSNPGQP VYYQVLNESL YEGGLGINYG 130 140 150 160 170 180 SNGIRRLDTV VSLAERYDIQ LVLTFMNNWN DFGGINIYSN AFGSNATTWY TDKKSQRAYR 190 200 210 220 230 240 EYIKFIVNRY KGSSAIFAWE LGNEPRCKGC DPSVIYNWAK SVSAYIKKLD KKHMVALGDE 250 260 270 280 290 300 GWLCPPEGDG TYAYDCSEGV DFVKNLEIET LDYGTFHLYP ESWGYNYSWG SEWVLQHDAI 310 320 330 340 350 360 GKRFNKPVVF EEYGTPLNHT QLERPWQLTT VKETQVAADF IWQFGTVLPV EGTEWGDVNS 370 380 IYYGTEEYEV LAVQHAWEMA RKKVPRH

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	DQ490485 mRNA. Translation: ABF50861.1. AACD01000055 Genomic DNA. Translation: EAA63265.1. Sequence problems. BN001306 Genomic DNA. Translation: CBF83007.1. Sequence problems.
RefSeq	XP_660901.1. XM_655809.1.
3D structure databases
ProteinModelPortal	Q5B833.
ModBase	Search...
Protein family/group databases
mycoCLAP	MAN5A_EMENI.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADANIAT00009761; CADANIAP00009761; CADANIAG00009761.
GeneID	2873762.
KEGG	ani:AN3297.2.
Phylogenomic databases
eggNOG	COG3934.
HOGENOM	HOG000169951.
OrthoDB	EOG4XSPZK.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR001547. Glyco_hydro_5. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00150. Cellulase. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00659. GLYCOSYL_HYDROL_F5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANB_EMENI

Accession

Primary (citable) accession number: Q5B833
Secondary accession number(s): C8VI04, Q1HFT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	April 20, 2010
Last modified:	May 1, 2013
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program