P55296 (MANA_PIRSP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
1,4-beta-D-mannan mannanohydrolase A
Beta-mannanase A

Gene names

Name:

MANA

Organism

Piromyces sp.

Taxonomic identifier

45796 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Neocallimastigomycota › Neocallimastigomycetes › Neocallimastigales › Neocallimastigaceae › Piromyces

Protein attributes

Sequence length	606 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	Hydrolyzes 1,4-beta linked polysaccharide backbones of mannans, one of the major hemicellulose components in hardwoods and softwoods. Shows very high activity against mannohexaose but not against mannopentaose and smaller mannooligosaccharides. The major products released from mannooligosaccharide hydrolysis are mannose and mannobiose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.
Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Domain	Consists of a catalytic N-terminal domain linked to a reiterated non-catalytic C-terminal domain.
Sequence similarities	Belongs to the glycosyl hydrolase 26 family. Contains 1 CBM6 (carbohydrate binding type-6) domain.

Ontologies

Keywords
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological process	substituted mannan metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro cellulase activity 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 – 19	19	Potential
	Chain	20 – 606	587	Mannan endo-1,4-beta-mannosidase A		PRO_0000012174
Regions
	Domain	22 – 140	119	CBM6
	Repeat	490 – 528	39	1
	Repeat	529 – 567	39	2
	Repeat	568 – 606	39	3
	Region	141 – 471	331	Catalytic
	Region	472 – 489	18	Linker
	Region	490 – 606	117	3 X 39 AA approximate tandem repeats

Sequences

	Sequence		Length	Mass (Da)
	P55296 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 79AAFEEFA2725D86	FASTA	606	68,055
	10 20 30 40 50 60 MKSLNVILTL LSLIISVLSK KVYYEAEDGK LNGITVFKEL SGFSGKGYVG RFENPGNSVT 70 80 90 100 110 120 VTVDAPATGM YDLSIIYCAN MGQKINSLTV NDQSVGDITF TENTKFETKD VGAVYLNKGK 130 140 150 160 170 180 NTIGLVSSWG WMWVDAFVIN DAPNAAKDVS SKLNPTLVNP KAIPAAKKLY DFLKTNYGKR 190 200 210 220 230 240 ILSGQVGAAG QAGDEGQEIQ RIQKATGKLP AVWNMDFIFE SNDCTWRPQN PDITEMAINW 250 260 270 280 290 300 WKKYEGKGIM AAQWHWNIAG KTGDFAFYSK DTTFNLENAV TEGTWEYEKI IKDIDRVSGH 310 320 330 340 350 360 IKKLQAVNMP LIWRPLHENN GDWFWWGNNP KACAKLWKIL YERMVNYHGL NNLIWLWNGN 370 380 390 400 410 420 NDANTPVDYI DIIGVDIYAN DHGPQTTAYN THFDFYGGKK MVVLSENGRI PDIQQCVDQD 430 440 450 460 470 480 VWWGYFQTWN SEFILQDSYH TDAQLKEYFN HKTVMNMDEL PSFNVDSYNG DSGSSHNGNS 490 500 510 520 530 540 ESNSNTGNSD ECWSINLGYP CCIGDYVVTT DENGDWGVEN NEWCGIVHKS CWSEPLGYPC 550 560 570 580 590 600 CVGNTVISAD ESGDWGVENN EWCGIVHKSC WAEFLGYPCC VGNTVISTDE FGDWGVENDD WCGILN

References

[1]

"The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain." Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J. J. Biol. Chem. 270:29314-29322(1995) [PubMed: 7493964] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X91857 mRNA. Translation: CAA62968.1.
3D structure databases
ProteinModelPortal	P55296.
ModBase	Search...
Protein family/group databases
CAZy	CBM35. Carbohydrate-Binding Module Family 35. GH26. Glycoside Hydrolase Family 26.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002883. CBM10/Dockerin_dom. IPR005084. CMB_fam6. IPR009034. Dockerin_dom. IPR022790. EndoGluc_H/Glyco_hydro_26. IPR008979. Galactose-bd-like. IPR000805. Glyco_hydro_26. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.90.1220.10. Dockerin_CBD_5. 3 hits. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF02013. CBM_10. 3 hits. PF02156. Glyco_hydro_26. 1 hit. [Graphical view]
PRINTS	PR00739. GLHYDRLASE26.
SUPFAM	SSF64571. Dockering_CDD. 3 hits. SSF49785. Gal_bind_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS51175. CBM6. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANA_PIRSP

Accession

Primary (citable) accession number: P55296

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program