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P19424

- GUN_BACS6

UniProt

P19424 - GUN_BACS6

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Protein

Endoglucanase

Gene
N/A
Organism
Bacillus sp. (strain KSM-635)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei373 – 3731Proton donor
Active sitei485 – 4851Nucleophile

GO - Molecular functioni

  1. cellulase 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

CAZyiCBM17. Carbohydrate-Binding Module Family 17.
CBM28. Carbohydrate-Binding Module Family 28.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoglucanase (EC:3.2.1.4)
Alternative name(s):
Alkaline cellulase
Endo-1,4-beta-glucanase
OrganismiBacillus sp. (strain KSM-635)
Taxonomic identifieri1415 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Add
BLAST
Chaini30 – 941912EndoglucanasePRO_0000007838Add
BLAST

Structurei

Secondary structure

1
941
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi232 – 2354
Beta strandi239 – 2435
Beta strandi246 – 2505
Beta strandi254 – 2563
Beta strandi260 – 2656
Helixi267 – 2704
Helixi271 – 2733
Helixi276 – 2838
Beta strandi289 – 30113
Turni302 – 3043
Helixi308 – 32114
Beta strandi325 – 3317
Beta strandi334 – 3363
Helixi341 – 3433
Helixi346 – 35712
Helixi363 – 3653
Beta strandi366 – 3694
Helixi388 – 40821
Beta strandi413 – 4153
Helixi418 – 4214
Helixi424 – 4296
Beta strandi433 – 44412
Turni445 – 4473
Helixi461 – 4633
Helixi467 – 47610
Beta strandi481 – 49010
Turni491 – 4933
Helixi499 – 51113
Beta strandi516 – 5216
Beta strandi524 – 5263
Turni536 – 5383
Helixi554 – 5563
Helixi559 – 56911

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G01X-ray1.90A228-584[»]
1G0CX-ray1.90A228-584[»]
ProteinModelPortaliP19424.
SMRiP19424. Positions 227-752, 759-941.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19424.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 9458SLH 1PROSITE-ProRule annotationAdd
BLAST
Domaini95 – 15864SLH 2PROSITE-ProRule annotationAdd
BLAST
Domaini161 – 22464SLH 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 3 SLH (S-layer homology) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR005086. CBM_fam_17/28.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. S-layer_homology_dom.
[Graphical view]
PfamiPF03424. CBM_17_28. 2 hits.
PF00150. Cellulase. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51272. SLH. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P19424-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKIKQIKQSL SLLLIITLIM SLFVPMASAN TNESKSNAFP FSDVKKTSWS
60 70 80 90 100
FPYIKDLYEQ EVITGTSATT FSPTDSVTRA QFTVMLTRGL GLEASSKDYP
110 120 130 140 150
FKDRKNWAYK EIQAAYEAGI VTGKTNGEFA PNENITREQM AAMAVRAYEY
160 170 180 190 200
LENELSLPEE QREYNDSSSI STFAQDAVQK AYVLELMEGN TDGYFQPKRN
210 220 230 240 250
STREQSAKVI STLLWKVASH DYLYHTEAVK SPSEAGALQL VELNGQLTLA
260 270 280 290 300
GEDGTPVQLR GMSTHGLQWF GEIVNENAFV ALSNDWGSNM IRLAMYIGEN
310 320 330 340 350
GYATNPEVKD LVYEGIELAF EHDMYVIVDW HVHAPGDPRA DVYSGAYDFF
360 370 380 390 400
EEIADHYKDH PKNHYIIWEL ANEPSPNNNG GPGLTNDEKG WEAVKEYAEP
410 420 430 440 450
IVEMLREKGD NMILVGNPNW SQRPDLSADN PIDAENIMYS VHFYTGSHGA
460 470 480 490 500
SHIGYPEGTP SSERSNVMAN VRYALDNGVA VFATEWGTSQ ANGDGGPYFD
510 520 530 540 550
EADVWLNFLN KHNISWANWS LTNKNEISGA FTPFELGRTD ATDLDPGANQ
560 570 580 590 600
VWAPEELSLS GEYVRARIKG IEYTPIDRTK FTKLVWDFND GTTQGFQVNG
610 620 630 640 650
DSPNKESITL SNNNDALQIE GLNVSNDISE GNYWDNVRLS ADGWSENVDI
660 670 680 690 700
LGATELTIDV IVEEPTTVSI AAIPQGPAAG WANPTRAIKV TEDDFESFGD
710 720 730 740 750
GYKALVTITS EDSPSLETIA TSPEDNTMSN IILFVGTEDA DVISLDNITV
760 770 780 790 800
SGTEIEIEVI HDEKGTATLP STFEDGTRQG WDWHTESGVK TALTIEEANG
810 820 830 840 850
SNALSWEYAY PEVKPSDGWA TAPRLDFWKD ELVRGTSDYI SFDFYIDAVR
860 870 880 890 900
ASEGAISINA VFQPPANGYW QEVPTTFEID LTELDSATVT SDELYHYEVK
910 920 930 940
INIRDIEAIT DDTELRNLLL IFADEDSDFA GRVFVDNVRF E
Length:941
Mass (Da):104,628
Last modified:November 1, 1990 - v1
Checksum:iBEA2AC3B169BFADA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27420 Genomic DNA. Translation: AAA22304.1.
PIRiS29043.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M27420 Genomic DNA. Translation: AAA22304.1 .
PIRi S29043.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G01 X-ray 1.90 A 228-584 [» ]
1G0C X-ray 1.90 A 228-584 [» ]
ProteinModelPortali P19424.
SMRi P19424. Positions 227-752, 759-941.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM17. Carbohydrate-Binding Module Family 17.
CBM28. Carbohydrate-Binding Module Family 28.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P19424.

Family and domain databases

Gene3Di 2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProi IPR005086. CBM_fam_17/28.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. S-layer_homology_dom.
[Graphical view ]
Pfami PF03424. CBM_17_28. 2 hits.
PF00150. Cellulase. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51272. SLH. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and nucleotide sequence of a gene for alkaline cellulase from Bacillus sp. KSM-635."
    Ozaki K., Shikata S., Kawai S., Ito S., Okamoto K.
    J. Gen. Microbiol. 136:1327-1334(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Crystallization and preliminary X-ray analysis of a truncated family A alkaline endoglucanase isolated from Bacillus sp. KSM-635."
    Shirai T., Yamane T., Hidaka T., Kuyama K., Suzuki A., Ashida T., Ozaki K., Ito S.
    J. Biochem. 122:683-685(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 228-584, CRYSTALLIZATION.
  3. "Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme."
    Shirai T., Ishida H., Noda J., Yamane T., Ozaki K., Hakamada Y., Ito S.
    J. Mol. Biol. 310:1079-1087(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 221-584.

Entry informationi

Entry nameiGUN_BACS6
AccessioniPrimary (citable) accession number: P19424
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: October 1, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3