Reviewed, UniProtKB/Swiss-Prot P51529 (MANA_STRLI)

Names and origin

Protein names

Recommended name:
    Mannan endo-1,4-beta-mannosidase
    EC=3.2.1.78
Alternative name(s):
    Beta-mannanase
    1,4-beta-D-mannan mannanohydrolase

Gene names

Name:

manA

Organism

Streptomyces lividans

Taxonomic identifier

1916 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	383 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)

Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Subunit structure	Monomer.
Sequence similarities	Belongs to the glycosyl hydrolase 5 (cellulase A) family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.8. Temperature dependence: Optimum temperature is 58 degrees Celsius.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cation 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 – 35	35	Ref.1
	Chain	36 – 383	348	Mannan endo-1,4-beta-mannosidase		PRO_0000007900
Regions
	Compositional bias	336 – 340	5	Poly-Gly

Sequences

	Sequence		Length	Mass (Da)
	P51529-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 5DB4B407C64E94C3	FASTA	383	39,682
	10 20 30 40 50 60 MRNARSTLIT TAGMAFAVLG LLFALAGPSA GRAEAAAGGI HVSNGRVVEG NGSAFVMRGV 70 80 90 100 110 120 NHAYTWYPDR TGSIADIAAK GANTVRVVLS SGGRWTKTSA SEVSALIGQC KANKVICVLE 130 140 150 160 170 180 VHDTTGYGKD GATSLDQAGD YWVGVKSAAW RAQEDYVVVN IGNEPFGNTN YAAWTDATKS 190 200 210 220 230 240 AIGKLRGAGL GHALMVDAPN WGQDWSGTMR SNAASVFASD PDRNTVFSIH MYGVYDTAAE 250 260 270 280 290 300 VRDYLNAFVG NGLPIVVGEF GDQHSDGNPD EDAIMATAQS LGVGYLGWSW SGNGGGVEYL 310 320 330 340 350 360 DMVNGFDPNS LTSWGNRILY GSNGIAATSR TATVYGGGGG STGGTAPNGY PYCVNGGASD 370 380 PDGDGWGWEN SRSCVVRGSA ADH

References

[1]	"Beta-mannanase of Streptomyces lividans 66: cloning and DNA sequence of the manA gene and characterization of the enzyme." Arcand N., Kluepfel D., Paradis F.W., Morosoli R., Shareck F. Biochem. J. 290:857-863(1993) [PubMed: 8457214] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-42. Strain: 66 / 1326.
[2]	Shareck F. Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M92297 Genomic DNA. Translation: AAA26710.2.
PIR	S30386.
3D structure databases
SMR	P51529. Positions 37-336.
ModBase	Search...
Protein family/group databases
CAZy	CBM10. Carbohydrate-Binding Module Family 10. GH5. Glycoside Hydrolase Family 5.
Enzyme and pathway databases
BRENDA	3.2.1.78. 15238.
Family and domain databases
InterPro	IPR002883. Dockerin_cellulose-bd_dom. IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR017853. Glyco_hydro_catalytic_core. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF02013. CBM_10. 1 hit. PF00150. Cellulase. 1 hit. [Graphical view]
PROSITE	PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANA_STRLI

Accession

Primary (citable) accession number: P51529

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 30, 2000
Last modified:	January 19, 2010
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)