Q4WBS1 (MANF_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	manF
ORF Names:	AFUA_8G07030

Organism

Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]

Taxonomic identifier

330879 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	438 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Ref.2 Ref.3
Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Subcellular location	Secreted By similarity.
Domain	Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in serines, and a C-terminal endo-1,4-mannanase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family. Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.
Biophysicochemical properties	Kinetic parameters: KM=3.07 mM for locust bean galactomannan Ref.2 Ref.3 Vmax=1935 µmol/min/mg enzyme pH dependence: Optimum pH is 4.0 to 5.0. Temperature dependence: Optimum temperature is 65 degrees Celsius. Stable up to 55 degrees Celsius.
Sequence caution	The sequence EAL85463.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cellulose binding Inferred from electronic annotation. Source: InterPro mannan endo-1,4-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 – 17	17	Ref.2
	Chain	18 – 438	421	Mannan endo-1,4-beta-mannosidase F		PRO_0000393715
Regions
	Domain	19 – 54	36	CBM1
	Region	60 – 96	37	Ser-rich linker
	Region	97 – 438	342	Catalytic
Sites
	Active site	264	1	Proton donor By similarity
	Active site	373	1	Nucleophile By similarity
Amino acid modifications
	Glycosylation	277	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	14 – 17	4	GAVA → IYGS in ACH58410. Ref.2
	Sequence conflict	83	1	A → S in ACH58411. Ref.3
	Sequence conflict	234 – 236	3	KIQ → QIP in ACH58411. Ref.3
	Sequence conflict	254	1	P → L in ACH58411. Ref.3
	Sequence conflict	279	1	T → A in ACH58411. Ref.3
	Sequence conflict	385	1	L → P in ACH58411. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q4WBS1 [UniParc]. Last modified April 20, 2010. Version 2. Checksum: 8E55123506BD7E24	FASTA	438	47,327
	10 20 30 40 50 60 MHPLPSVALL SAIGAVAAQV GPWGQCGGRS YTGETSCVSG WSCVLFNEWY SQCQPATTTS 70 80 90 100 110 120 TSSVSATAAP SSTSSSKESV PSATTSKKPV PTGSSSFVKA DGLKFNIDGE TKYFAGTNAY 130 140 150 160 170 180 WLPFLTNDAD VDSVMDNLQK AGLKILRTWG FNDVNSKPSS GTVYFQLHDP STGTTTINTG 190 200 210 220 230 240 ADGLQRLDYV VSAAEKRGIK LLIPLVNNWD DYGGMNAYVK AYGGSKTEWY TNSKIQSVYQ 250 260 270 280 290 300 AYIKAVVSRY RDSPAIMAWE LSNEARCQGC STDVIYNWTA KTSAYIKSLD PNHMVATGDE 310 320 330 340 350 360 GMGVTVDSDG SYPYSTYEGS DFAKNLAAPD IDFGVFHLYT EDWGIKDNSW GNGWVTSHAK 370 380 390 400 410 420 VCKAAGKPCL FEEYGLKDDH CSASLTWQKT SVSSGMAADL FWQYGQTLST GPSPNDHFTI 430 YYGTSDWQCG VADHLSTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus." Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W. Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[2]	"Purification and characterization of two forms of endo-beta-1,4-mannanase from a thermotolerant fungus, Aspergillus fumigatus IMI 385708 (formerly Thermomyces lanuginosus IMI 158749)." Puchart V., Vrsanska M., Svoboda P., Pohl J., Ogel Z.B., Biely P. Biochim. Biophys. Acta 1674:239-250(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-438, PROTEIN SEQUENCE OF 18-29; 113-133 AND 325-347, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: IMI 385708.
[3]	"Cloning, expression and characterization of endo-beta-1,4-mannanase from Aspergillus fumigatus in Aspergillus sojae and Pichia pastoris." Duruksu G., Ozturk B., Biely P., Bakir U., Ogel Z.B. Biotechnol. Prog. 25:271-276(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-438, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: IMI 385708.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAHF01000013 Genomic DNA. Translation: EAL85463.1. Different initiation. EU925594 Genomic DNA. Translation: ACH58410.1. EU925595 mRNA. Translation: ACH58411.1.
RefSeq	XP_747501.1. XM_742408.1.
3D structure databases
ProteinModelPortal	Q4WBS1.
ModBase	Search...
Protein family/group databases
CAZy	CBM1. Carbohydrate-Binding Module Family 1. GH5. Glycoside Hydrolase Family 5.
mycoCLAP	MAN5A_ASPFU.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	CADAFUAT00003026; CADAFUAP00003026; CADAFUAG00003026.
GeneID	3504904.
KEGG	afm:AFUA_8G07030.
Phylogenomic databases
eggNOG	COG3934.
HOGENOM	HOG000169951.
KO	K01567.
OrthoDB	EOG44BF9Z.
Family and domain databases
Gene3D	3.20.20.80. 1 hit.
InterPro	IPR000254. Cellulose-bd_dom_fun. IPR001547. Glyco_hydro_5. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00734. CBM_1. 1 hit. PF00150. Cellulase. 1 hit. [Graphical view]
SMART	SM00236. fCBD. 1 hit. [Graphical view]
SUPFAM	SSF57180. CBD_fun. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00562. CBM1_1. 1 hit. PS51164. CBM1_2. 1 hit. PS00659. GLYCOSYL_HYDROL_F5. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANF_ASPFU

Accession

Primary (citable) accession number: Q4WBS1
Secondary accession number(s): B5LZ77, B5LZ78

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 20, 2010
Last sequence update:	April 20, 2010
Last modified:	May 1, 2013
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program