Reviewed, UniProtKB/Swiss-Prot P22533 (MANB_CALSA)

Names and origin

Protein names

Recommended name:
    Beta-mannanase/endoglucanase A
Including the following 2 domains:
    1- Recommended name:
            Mannan endo-1,4-beta-mannosidase A
              EC=3.2.1.78
        Alternative name(s):
            Beta-mannanase
            Endo-1,4-mannanase
    2- Recommended name:
            Endo-1,4-beta-glucanase
              EC=3.2.1.4
        Alternative name(s):
            Cellulase

Gene names

Name:

manA

Organism

Caldocellum saccharolyticum (Caldicellulosiruptor saccharolyticus)

Taxonomic identifier

44001 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacterales Family III. Incertae Sedis › Caldicellulosiruptor

Protein attributes

Sequence length	1331 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	Degradation of hemicelluloses, the second most abundant polysaccharides in nature. Contains two catalytic domains with mannanase and endoglucanase activities.
Catalytic activity	Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans. Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence similarities	In the N-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family. In the C-terminal section; belongs to the glycosyl hydrolase 44 (cellulase J) family. Contains 2 CBM3 (carbohydrate binding type-3) domains.
biophysicochemical properties	pH dependence: Optimum pH is 6. Temperature dependence: Optimum temperature is 80 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Cellulose degradation Polysaccharide degradation
Domain	Repeat Signal
Molecular function	Glycosidase Hydrolase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
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: EC 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 – 41	41	Potential
	Chain	42 – 1331	1290	Beta-mannanase/endoglucanase A		PRO_0000007899
Regions
	Domain	363 – 516	154	CBM3 1
	Domain	566 – 719	154	CBM3 2
	Region	42 – 325	284	Catalytic (mannanase)
	Region	781 – 1331	551	Catalytic (endoglucanase)
	Compositional bias	326 – 361	36	Pro/Ser/Thr-rich (PT box)
	Compositional bias	519 – 564	46	Pro/Ser/Thr-rich (PT box)
	Compositional bias	721 – 780	60	Pro/Ser/Thr-rich (PT box)
Sites
	Active site	162	1	Proton donor By similarity
	Active site	257	1	Nucleophile By similarity
Experimental info
	Sequence conflict	338	1	T → P Ref.2
	Sequence conflict	340 – 346	7	TPTPTPT → RQHQHRQ Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P22533-1 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: FFBCA51BB8D8F0E0	FASTA	1,331	146,893
	10 20 30 40 50 60 MRLKTKIRKK WLSVLCTVVF LLNILFIANV TILPKVGAAT SNDGVVKIDT STLIGTNHAH 70 80 90 100 110 120 CWYRDRLDTA LRGIRSWGMN SVRVVLSNGY RWTKIPASEV ANIISLSRSL GFKAIILEVH 130 140 150 160 170 180 DTTGYGEDGA ACSLAQAVEY WKEIKSVLDG NEDFVIINIG NEPYGNNNYQ NWVNDTKNAI 190 200 210 220 230 240 KALRDAGFKH TIMVDAPNWG QDWSNTMRDN AQSIMEADPL RNLVFSIHMY GVYNTASKVE 250 260 270 280 290 300 EYIKSFVDKG LPLVIGEFGH QHTDGDPDEE AIVRYAKQYK IGLFSWSWCG NSSYVGYLDM 310 320 330 340 350 360 VNNWDPNNPT PWGQWYKTNA IGTSSTPTPT STVTPTPTPT PTPTPTVTAT PTPTPTPVST 370 380 390 400 410 420 PATSGQIKVL YANKETNSTT NTIRPWLKVV NSGSSSIDLS RVTIRYWYTV DGERAQSAIS 430 440 450 460 470 480 DWAQIGASNV TFKFVKLSSS VSGADYYLEI GFKSGAGQLQ PGKDTGEIQM RFNKDDWSNY 490 500 510 520 530 540 NQGNDWSWIQ SMTSYGENEK VTAYIDGVLV WGQEPSGATP APAPTATPTP TPTVTPTPTV 550 560 570 580 590 600 TPTPTVTATP TPTPTPTPTP VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI 610 620 630 640 650 660 DLSRVTIRYW YTVDGERAQS AISDWAQIGA SNVTFKFVKL SSSVSGADYY LEIGFKSGAG 670 680 690 700 710 720 QLQPGKDTGE IQIRFNKSDW SNYNQGNDWS WIQSMTSYGE NEKVTAYIDG VLVWGQEPSG 730 740 750 760 770 780 TTPSPTSTPT VTVTPTPTPT PTPTPTPTVT PTPTVTPTPT VTATPTPTPT PIPTVTPLPT 790 800 810 820 830 840 ISPSPSVVEI TINTNAGRTQ ISPYIYGANQ DIEGVVHSAR RLGGNRLTGY NWENNFSNAG 850 860 870 880 890 900 NDWYHSSDDY LCWSMGISGE DAKVPAAVVS KFHEYSLKNN AYSAVTLQMA GYVSKDNYGT 910 920 930 940 950 960 VSENETAPSN RWAEVKFKKD APLSLNPDLN DNFVYMDEFI NYLINKYGMA SSPTGIKGYI 970 980 990 1000 1010 1020 LDNEPDLWAS THPRIHPNKV TCKELIEKSV ELAKVIKTLD PSAEVFGYAS YGFMGYYSLQ 1030 1040 1050 1060 1070 1080 DAPDWNQVKG EHRWFISWYL EQMKKASDSF GKRLLDVLDL HWYPEARGGN IRVCFDGEND 1090 1100 1110 1120 1130 1140 TSKEVVIARM QAPRTLWDPT YKTSVKGQIT AGENSWINQW FSDYLPIIPN VKADIEKYYP 1150 1160 1170 1180 1190 1200 GTKLAISEFD YGGRNHISGG IALADVLGIF GKYGVNFAAR WGDSGSYAAA AYNIYLNYDG 1210 1220 1230 1240 1250 1260 KGSKYGNTNV SANTSDVENM PVYASINGQD DSELHIILIN RNYDQKLQVK INITSTPKYT 1270 1280 1290 1300 1310 1320 KAEIYGFDSN SPEYKKMGNI DNIESNVFTL EVPKFNGVSH SITLDFNVSI KIIQNEVIKF 1330 IRNLVFMRAL V

References

[1]	"The beta-mannanase from 'Caldocellum saccharolyticum' is part of a multidomain enzyme." Gibbs M.D., Saul D.J., Luthi E., Bergquist P.L. Appl. Environ. Microbiol. 58:3864-3867(1992) [PubMed: 1476429] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning, sequence analysis, and expression in Escherichia coli of a gene coding for a beta-mannanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum'." Luethi E., Jasmat N.B., Grayling R.A., Love D.R., Bergquist P.L. Appl. Environ. Microbiol. 57:694-700(1991) [PubMed: 2039230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L01257 Unassigned DNA. Translation: AAA71887.1. M36063 Genomic DNA. Translation: AAA72861.1.
PIR	A48954.
3D structure databases
HSSP	HSSP built from PDB template 1NBC based on UniProtKB Q06851.
ModBase	Search...
Protein family/group databases
CAZy	CBM3. Carbohydrate-Binding Module Family 3. GH44. Glycoside Hydrolase Family 44. GH5. Glycoside Hydrolase Family 5.
Enzyme and pathway databases
BRENDA	3.2.1.4. 15230. 3.2.1.78. 15230.
Family and domain databases
InterPro	IPR001956. CBD_3. IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR013781. Glyco_hydro_sg_catalytic. [Graphical view]
Gene3D	G3DSA:2.60.40.710. CBD_3. 2 hits. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00942. CBM_3. 2 hits. PF00150. Cellulase. 1 hit. [Graphical view]
ProDom	PD001947. CBD_3. 2 hits. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS51172. CBM3. 2 hits. PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MANB_CALSA

Accession

Primary (citable) accession number: P22533

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 72 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)