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Protein

Beta-mannanase/endoglucanase A

Gene

manA

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei162Proton donorBy similarity1
Active sitei257NucleophileBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase, Multifunctional enzyme
Biological processCarbohydrate 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 41Sequence analysisAdd BLAST41
ChainiPRO_000000789942 – 1331Beta-mannanase/endoglucanase AAdd BLAST1290

Structurei

3D structure databases

ProteinModelPortaliP22533
SMRiP22533
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini363 – 516CBM3 1PROSITE-ProRule annotationAdd BLAST154
Domaini566 – 719CBM3 2PROSITE-ProRule annotationAdd BLAST154

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 325Catalytic (mannanase)Add BLAST284
Regioni781 – 1331Catalytic (endoglucanase)Add BLAST551

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi326 – 361Pro/Ser/Thr-rich (PT box)Add BLAST36
Compositional biasi519 – 564Pro/Ser/Thr-rich (PT box)Add BLAST46
Compositional biasi721 – 780Pro/Ser/Thr-rich (PT box)Add BLAST60

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4106R7G Bacteria
COG2730 LUCA

Family and domain databases

Gene3Di2.60.40.1180, 2 hits
2.60.40.710, 2 hits
InterProiView protein in InterPro
IPR008965 CBM2/CBM3_carb-bd_dom_sf
IPR001956 CBM3
IPR036966 CBM3_sf
IPR024745 Glyco_hydro_44
IPR001547 Glyco_hydro_5
IPR018087 Glyco_hydro_5_CS
IPR013780 Glyco_hydro_b
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00942 CBM_3, 2 hits
PF00150 Cellulase, 1 hit
PF12891 Glyco_hydro_44, 1 hit
SMARTiView protein in SMART
SM01067 CBM_3, 2 hits
SUPFAMiSSF49384 SSF49384, 2 hits
SSF51445 SSF51445, 3 hits
PROSITEiView protein in PROSITE
PS51172 CBM3, 2 hits
PS00659 GLYCOSYL_HYDROL_F5, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti338T → P (PubMed:2039230).Curated1
Sequence conflicti340 – 346TPTPTPT → RQHQHRQ (PubMed:2039230).Curated7

Sequence databases

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

Similar proteinsi

Entry informationi

Entry nameiMANB_CALSA
AccessioniPrimary (citable) accession number: P22533
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 1, 1993
Last modified: March 28, 2018
This is version 108 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health