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P22533

- MANB_CALSA

UniProt

P22533 - MANB_CALSA

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Protein

Beta-mannanase/endoglucanase A

Gene

manA

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Degradation of hemicelluloses, the second most abundant polysaccharides in nature. Contains two catalytic domains with mannanase and endoglucanase activities.

Catalytic activityi

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.

pH dependencei

Optimum pH is 6.

Temperature dependencei

Optimum temperature is 80 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621Proton donorBy similarity
Active sitei257 – 2571NucleophileBy similarity

GO - Molecular functioni

  1. cellulase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro
  3. mannan endo-1,4-beta-mannosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Protein family/group databases

CAZyiCBM3. Carbohydrate-Binding Module Family 3.
GH44. Glycoside Hydrolase Family 44.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-mannanase/endoglucanase A
Including the following 2 domains:
Mannan endo-1,4-beta-mannosidase A (EC:3.2.1.78)
Alternative name(s):
Beta-mannanase
Endo-1,4-mannanase
Endo-1,4-beta-glucanase (EC:3.2.1.4)
Alternative name(s):
Cellulase
Gene namesi
Name:manA
OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic identifieri44001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Sequence AnalysisAdd
BLAST
Chaini42 – 13311290Beta-mannanase/endoglucanase APRO_0000007899Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP22533.
SMRiP22533. Positions 786-1298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini363 – 516154CBM3 1PROSITE-ProRule annotationAdd
BLAST
Domaini566 – 719154CBM3 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 325284Catalytic (mannanase)Add
BLAST
Regioni781 – 1331551Catalytic (endoglucanase)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi326 – 36136Pro/Ser/Thr-rich (PT box)Add
BLAST
Compositional biasi519 – 56446Pro/Ser/Thr-rich (PT box)Add
BLAST
Compositional biasi721 – 78060Pro/Ser/Thr-rich (PT box)Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyl hydrolase 5 (cellulase A) family.Curated
In the C-terminal section; belongs to the glycosyl hydrolase 44 (cellulase J) family.Curated
Contains 2 CBM3 (carbohydrate binding type-3) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2730.

Family and domain databases

Gene3Di2.60.40.710. 2 hits.
3.20.20.80. 3 hits.
InterProiIPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR024745. Glyco_hydro_44.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00942. CBM_3. 2 hits.
PF00150. Cellulase. 1 hit.
PF12891. Glyco_hydro_44. 1 hit.
[Graphical view]
SMARTiSM01067. CBM_3. 2 hits.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 2 hits.
SSF51445. SSF51445. 3 hits.
PROSITEiPS51172. CBM3. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P22533-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLKTKIRKK WLSVLCTVVF LLNILFIANV TILPKVGAAT SNDGVVKIDT
60 70 80 90 100
STLIGTNHAH CWYRDRLDTA LRGIRSWGMN SVRVVLSNGY RWTKIPASEV
110 120 130 140 150
ANIISLSRSL GFKAIILEVH DTTGYGEDGA ACSLAQAVEY WKEIKSVLDG
160 170 180 190 200
NEDFVIINIG NEPYGNNNYQ NWVNDTKNAI KALRDAGFKH TIMVDAPNWG
210 220 230 240 250
QDWSNTMRDN AQSIMEADPL RNLVFSIHMY GVYNTASKVE EYIKSFVDKG
260 270 280 290 300
LPLVIGEFGH QHTDGDPDEE AIVRYAKQYK IGLFSWSWCG NSSYVGYLDM
310 320 330 340 350
VNNWDPNNPT PWGQWYKTNA IGTSSTPTPT STVTPTPTPT PTPTPTVTAT
360 370 380 390 400
PTPTPTPVST PATSGQIKVL YANKETNSTT NTIRPWLKVV NSGSSSIDLS
410 420 430 440 450
RVTIRYWYTV DGERAQSAIS DWAQIGASNV TFKFVKLSSS VSGADYYLEI
460 470 480 490 500
GFKSGAGQLQ PGKDTGEIQM RFNKDDWSNY NQGNDWSWIQ SMTSYGENEK
510 520 530 540 550
VTAYIDGVLV WGQEPSGATP APAPTATPTP TPTVTPTPTV TPTPTVTATP
560 570 580 590 600
TPTPTPTPTP VSTPATGGQI KVLYANKETN STTNTIRPWL KVVNSGSSSI
610 620 630 640 650
DLSRVTIRYW YTVDGERAQS AISDWAQIGA SNVTFKFVKL SSSVSGADYY
660 670 680 690 700
LEIGFKSGAG QLQPGKDTGE IQIRFNKSDW SNYNQGNDWS WIQSMTSYGE
710 720 730 740 750
NEKVTAYIDG VLVWGQEPSG TTPSPTSTPT VTVTPTPTPT PTPTPTPTVT
760 770 780 790 800
PTPTVTPTPT VTATPTPTPT PIPTVTPLPT ISPSPSVVEI TINTNAGRTQ
810 820 830 840 850
ISPYIYGANQ DIEGVVHSAR RLGGNRLTGY NWENNFSNAG NDWYHSSDDY
860 870 880 890 900
LCWSMGISGE DAKVPAAVVS KFHEYSLKNN AYSAVTLQMA GYVSKDNYGT
910 920 930 940 950
VSENETAPSN RWAEVKFKKD APLSLNPDLN DNFVYMDEFI NYLINKYGMA
960 970 980 990 1000
SSPTGIKGYI LDNEPDLWAS THPRIHPNKV TCKELIEKSV ELAKVIKTLD
1010 1020 1030 1040 1050
PSAEVFGYAS YGFMGYYSLQ DAPDWNQVKG EHRWFISWYL EQMKKASDSF
1060 1070 1080 1090 1100
GKRLLDVLDL HWYPEARGGN IRVCFDGEND TSKEVVIARM QAPRTLWDPT
1110 1120 1130 1140 1150
YKTSVKGQIT AGENSWINQW FSDYLPIIPN VKADIEKYYP GTKLAISEFD
1160 1170 1180 1190 1200
YGGRNHISGG IALADVLGIF GKYGVNFAAR WGDSGSYAAA AYNIYLNYDG
1210 1220 1230 1240 1250
KGSKYGNTNV SANTSDVENM PVYASINGQD DSELHIILIN RNYDQKLQVK
1260 1270 1280 1290 1300
INITSTPKYT KAEIYGFDSN SPEYKKMGNI DNIESNVFTL EVPKFNGVSH
1310 1320 1330
SITLDFNVSI KIIQNEVIKF IRNLVFMRAL V
Length:1,331
Mass (Da):146,893
Last modified:July 1, 1993 - v2
Checksum:iFFBCA51BB8D8F0E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti338 – 3381T → P(PubMed:2039230)Curated
Sequence conflicti340 – 3467TPTPTPT → RQHQHRQ(PubMed:2039230)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01257 Unassigned DNA. Translation: AAA71887.1.
M36063 Genomic DNA. Translation: AAA72861.1.
PIRiA48954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01257 Unassigned DNA. Translation: AAA71887.1 .
M36063 Genomic DNA. Translation: AAA72861.1 .
PIRi A48954.

3D structure databases

ProteinModelPortali P22533.
SMRi P22533. Positions 786-1298.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM3. Carbohydrate-Binding Module Family 3.
GH44. Glycoside Hydrolase Family 44.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG2730.

Family and domain databases

Gene3Di 2.60.40.710. 2 hits.
3.20.20.80. 3 hits.
InterProi IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR024745. Glyco_hydro_44.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00942. CBM_3. 2 hits.
PF00150. Cellulase. 1 hit.
PF12891. Glyco_hydro_44. 1 hit.
[Graphical view ]
SMARTi SM01067. CBM_3. 2 hits.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 2 hits.
SSF51445. SSF51445. 3 hits.
PROSITEi PS51172. CBM3. 2 hits.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346.

Entry informationi

Entry nameiMANB_CALSA
AccessioniPrimary (citable) accession number: P22533
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 1, 1993
Last modified: October 1, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3