Reviewed, UniProtKB/Swiss-Prot P49425 (MANA_RHOMR)

Names and origin

Protein names

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

Gene names

Name:

manA

Organism

Rhodothermus marinus (Rhodothermus obamensis)

Taxonomic identifier

29549 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Rhodothermaceae › Rhodothermus

Protein attributes

Sequence length	1021 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Acts as endo-acting enzyme with a requirement for at least five sugar moieties for effective catalytic activity. Hydrolyzes carob-galactomannan (locust bean gum) effectively and to a smaller extent guar gum, but not yeast mannan. Ref.1
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. Contains 1 CBM6 (carbohydrate binding type-6) domain.
biophysicochemical properties	pH dependence: Optimum pH is 5.4. Temperature dependence: Optimum temperature is 85 degrees Celsius.

Ontologies

Keywords
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 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
	Chain	1 – 1021	1021	Mannan endo-1,4-beta-mannosidase		PRO_0000057685
Regions
	Domain	480 – 600	121	CBM6

Sequences

	Sequence		Length	Mass (Da)
	P49425-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: A8F7B63109E0F715	FASTA	1,021	115,791
	10 20 30 40 50 60 MAGPHRSRAA GPPPFAVDEH VALEMVAFRG EVFAGHGLLA DQRLIAHTGR PALNAQRITQ 70 80 90 100 110 120 QKQRDQCRGQ RHRHHQGGRN LRKAHRTFHE HQSTQDQAHD APHGQQAKTG HEGLGHEHAQ 130 140 150 160 170 180 AQHQQGQSNV VDRQDGEPVE AQHQKDGAQR AGNAPAGRVE LEQQPVEAQH QQQEGDVRIG 190 200 210 220 230 240 KRRQNAFAPP ALDHVHGGPG RLQRHGLAVE RHVPAVQQHQ QRVQRGRQQI DHVLGHGLPG 250 260 270 280 290 300 RQRLAFRDGP RRPVGVASPV LGQRPCPGHR IVQNLFRHGI DPCRVGRCRR SPSELHGMGC 310 320 330 340 350 360 ADVRARGHGR HMRGQRDEHP GRGRPCARRR HVDDDRDRTP QEKLYDVARG LDEPARRVHF 370 380 390 400 410 420 DDEADRSVFR GLAQPAPDEP EGRRRDRLVL QRQSVNHRRG RLSRHRQQHQ PQQQRPHGNQ 430 440 450 460 470 480 AFLGKYEKRR RKPTACLKSL RRFPDKDAPV LYFVNQLEKT KRRMTLLLVW LIFTGVAGEI 490 500 510 520 530 540 RLEAEDGELL GVAVDSTLTG YSGRGYVTGF DAPEDSVRFS FEAPRGVYRV VFGVSFSSRF 550 560 570 580 590 600 ASYALRVDDW HQTGSLIKRG GGFFEASIGE IWLDEGAHTM AFQLMNGALD YVRLEPVSYG 610 620 630 640 650 660 PPARPPAQLS DSQATASAQA LFAFLLSEYG RHILAGQQQN PYRRDFDAIN YVRNVTGKEP 670 680 690 700 710 720 ALVSFDLIDY SPTREAHGVV HYQTPEDWIA WAGRDGIVSL MWHWNAPTDL IEDPSQDCYW 730 740 750 760 770 780 WYGFYTRCTT FDVAAALADT SSERYRLLLR DIDVIAAQLQ KFQQADIPVL WRPLHEAAGG 790 800 810 820 830 840 WFWWGAKGPE PFKQLWRLLY ERLVHHHGLH NLIWVYTHEP GAAEWYPGDA YVDIVGRDVY 850 860 870 880 890 900 ADDPDALMRS DWNELQTLFG GRKLVALTET GTLPDVEVIT DYGIWWSWFS IWTDPFLRDV 910 920 930 940 950 960 DPDRLTRVYH SERVLTRDEL PDWRSYVLHA TTVQPAGDLA LAVYPNPGAG RLHVEVGLPV 970 980 990 1000 1010 1020 AAPVVVEVFN LLGQRVFQYQ AGMQPAGLWR RAFELALAPG VYLVQVRAGN LVARRRWVSV R

References

[1]

"A highly thermostable endo-(1,4)-beta-mannanase from the marine bacterium Rhodothermus marinus." Politz O., Krah M., Thomsen K.K., Borriss R. Appl. Microbiol. Biotechnol. 53:715-721(2000) [PubMed: 10919332] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 43812 / R-10 / DSM 4252.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X90947 Genomic DNA. Translation: CAA62442.1.
PIR	T10748.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	CBM35. Carbohydrate-Binding Module Family 35. GH26. Glycoside Hydrolase Family 26.
Enzyme and pathway databases
BRENDA	3.2.1.78. 1132.
Family and domain databases
InterPro	IPR005084. CBM_6. 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.
PROSITE	PS51175. CBM6. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANA_RHOMR

Accession

Primary (citable) accession number: P49425

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	December 15, 1998
Last modified:	June 16, 2009
This is version 41 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)