Reviewed, UniProtKB/Swiss-Prot P49424 (MANA_PSEFL)

Names and origin

Protein names

Recommended name:
    Mannan endo-1,4-beta-mannosidase
    EC=3.2.1.78
Alternative name(s):
    Mannanase A

Gene names

Name:

manA

Organism

Pseudomonas fluorescens

Taxonomic identifier

294 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	423 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	Hydrolyzes mannan and galactomannan, but displays little activity towards other polysaccharides located in the plant cell wall. Preferentially hydrolyzes the larger oligosaccharides.
Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence similarities	Belongs to the glycosyl hydrolase 26 family.
biophysicochemical properties	pH dependence: Optimum pH is about 7.0.

Ontologies

Keywords
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	substituted mannan 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 – 31

31

Potential

Propeptide

32 – 38

7

Potential

PRO_0000012172

Chain

39 – 423

385

Mannan endo-1,4-beta-mannosidase

PRO_0000012173

Secondary structure

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423

Helix Strand Turn

Details...

Helix

56 – 68

13

Turn

69 – 71

3

Beta strand

73 – 78

6

Turn

79 – 82

4

Beta strand

91 – 93

3

Helix

96 – 101

6

Beta strand

106 – 111

6

Helix

112 – 114

3

Helix

125 – 133

9

Beta strand

137 – 141

5

Turn

147 – 149

3

Helix

150 – 152

3

Turn

156 – 159

4

Turn

169 – 171

3

Helix

178 – 193

16

Beta strand

205 – 208

4

Beta strand

215 – 218

4

Helix

227 – 242

16

Beta strand

249 – 254

6

Helix

264 – 268

5

Turn

274 – 276

3

Beta strand

278 – 280

3

Beta strand

283 – 286

4

Beta strand

288 – 290

3

Helix

292 – 312

21

Beta strand

320 – 323

4

Helix

325 – 329

5

Helix

337 – 347

11

Helix

351 – 353

3

Beta strand

355 – 359

5

Helix

385 – 389

5

Helix

392 – 401

10

Helix

408 – 410

3

Sequences

	Sequence		Length	Mass (Da)
	P49424-1 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: EFDAB597F10BA3DD	FASTA	423	47,487
	10 20 30 40 50 60 MKTITTARLP WAAQSFALGI CLIALLGCNH AANKSSASRA DVKPVTVKLV DSQATMETRS 70 80 90 100 110 120 LFAFMQEQRR HSIMFGHQHE TTQGLTITRT DGTQSDTFNA VGDFAAVYGW DTLSIVAPKA 130 140 150 160 170 180 EGDIVAQVKK AYARGGIITV SSHFDNPKTD TQKGVWPVGT SWDQTPAVVD SLPGGAYNPV 190 200 210 220 230 240 LNGYLDQVAE WANNLKDEQG RLIPVIFRLY HENTGSWFWW GDKQSTPEQY KQLFRYSVEY 250 260 270 280 290 300 LRDVKGVRNF LYAYSPNNFW DVTEANYLER YPGDEWVDVL GFDTYGPVAD NADWFRNVVA 310 320 330 340 350 360 NAALVARMAE ARGKIPVISE IGIRAPDIEA GLYDNQWYRK LISGLKADPD AREIAFLLVW 370 380 390 400 410 420 RNAPQGVPGP NGTQVPHYWV PANRPENINN GTLEDFQAFY ADEFTAFNRD IEQVYQRPTL IVK

References

[1]	"A non-modular endo-beta-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa." Braithwaite K.L., Black G.W., Hazlewood G.P., Ali B.R.S., Gilbert H.J. Biochem. J. 305:1005-1010(1995) [PubMed: 7848261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-48. Strain: Sp. Cellulosa.
[2]	Gilbert H.J. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 364-423.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X82179 Genomic DNA. Translation: CAA57670.2.

PIR

S53374.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GVY	X-ray	1.70	A	39-421	[»]
1GW1	X-ray	1.65	A	43-421	[»]
1J9Y	X-ray	1.85	A	39-423	[»]
1ODZ	X-ray	1.40	A/B	39-423	[»]
1R7O	X-ray	1.85	A	29-423	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH26. Glycoside Hydrolase Family 26.

Enzyme and pathway databases

BRENDA

3.2.1.78. 329.

Family and domain databases

InterPro

IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF02156. Glyco_hydro_26. 1 hit.
[Graphical view]

PRINTS

PR00739. GLHYDRLASE26.

ProtoNet

Search...

Entry information

Entry name

MANA_PSEFL

Accession

Primary (citable) accession number: P49424

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	July 5, 2005
Last modified:	June 16, 2009
This is version 51 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)