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Protein

Endoglucanase

Gene

Athe_1867

Organism
Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) (Anaerocellum thermophilum)
Status
Unreviewed-Annotation score: Annotation score: 2 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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1307 – 13071Calcium; via carbonyl oxygenCombined sources
Metal bindingi1312 – 13121CalciumCombined sources
Metal bindingi1531 – 15311CalciumCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradationUniRule annotation, Polysaccharide degradation

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BioCyciCBES521460:GH8H-1905-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
EndoglucanaseUniRule annotation (EC:3.2.1.4UniRule annotation)
Gene namesi
Ordered Locus Names:Athe_1867Imported
OrganismiCaldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) (Anaerocellum thermophilum)Imported
Taxonomic identifieri521460 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor
Proteomesi
  • UP000007723 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi521460.Athe_1867.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EL8X-ray2.45A1126-1759[»]
4L0GX-ray2.00A1122-1759[»]
4L6XX-ray1.70A1122-1759[»]
4TXTX-ray2.00A1122-1759[»]
ProteinModelPortaliB9MKU7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini486 – 646161CBM3 (carbohydrate binding type-3)InterPro annotationAdd
BLAST
Domaini716 – 869154CBM3 (carbohydrate binding type-3)InterPro annotationAdd
BLAST
Domaini915 – 1068154CBM3 (carbohydrate binding type-3)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 9 (cellulase E) family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CYP. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000269731.
OMAiYRRIIAM.
OrthoDBiEOG6KQ6BP.

Family and domain databases

Gene3Di1.50.10.10. 5 hits.
2.60.40.710. 3 hits.
4.10.870.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR018221. Glyco_hydro_9_His_AS.
[Graphical view]
PfamiPF00942. CBM_3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
PRINTSiPR00844. GLHYDRLASE48.
SMARTiSM01067. CBM_3. 3 hits.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
SSF49384. SSF49384. 3 hits.
PROSITEiPS51172. CBM3. 3 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

B9MKU7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRYRRIIAM VVTFIFILGV VYGVKPWQEV RAGSFNYGEA LQKAIMFYEF
60 70 80 90 100
QMSGKLPNWV RNNWRGDSAL KDGQDNGLDL TGGWFDAGDH VKFNLPMSYT
110 120 130 140 150
GTMLSWAVYE YKDAFVKSGQ LEHILNQIEW VNDYFVKCHP SKYVYYYQVG
160 170 180 190 200
DGSKDHAWWG PAEVMQMERP SFKVTQSSPG STVVAETAAS LAAASIVLKD
210 220 230 240 250
RNPTKAATYL QHAKELYEFA EVTKSDAGYT AANGYYNSWS GFYDELSWAA
260 270 280 290 300
VWLYLATNDS TYLTKAESYV QNWPKISGSN TIDYKWAHCW DDVHNGAALL
310 320 330 340 350
LAKITGKDIY KQIIESHLDY WTTGYNGERI KYTPKGLAWL DQWGSLRYAT
360 370 380 390 400
TTAFLAFVYS DWVGCPSTKK EIYRKFGESQ IDYALGSAGR SFVVGFGTNP
410 420 430 440 450
PKRPHHRTAH SSWADSQSIP SYHRHTLYGA LVGGPGSDDS YTDDISNYVN
460 470 480 490 500
NEVACDYNAG FVGALAKMYQ LYGGNPIPDF KAIETPTNDE FFVEAGINAS
510 520 530 540 550
GTNFIEIKAI VNNQSGWPAR ATDKLKFRYF VDLSELIKAG YSPNQLTLST
560 570 580 590 600
NYNQGAKVSG PYVWDASKNI YYILVDFTGT LIYPGGQDKY KKEVQFRIAA
610 620 630 640 650
PQNVQWDNSN DYSFQDIKGV SSGSVVKTKY IPLYDGDVKV WGEEPGTSGA
660 670 680 690 700
TPTPTATATP TPTPTVTPTP TPTPTSTATP TPTPTPTVTP TPTPTPTATP
710 720 730 740 750
TATPTPTSTP SSTPVAGGQI KVLYANKETN STTNTIRPWL KVVNTGSSSI
760 770 780 790 800
DLSRVTIRYW YTVDGDKAQS AISDWAQIGA SNVTFKFVKL SSSVSGADYY
810 820 830 840 850
LEIGFKSGAG QLQAGKDTGE IQIRFNKSDW SNYNQGNDWS WMQSMTNYGE
860 870 880 890 900
NVKVTAYIDG VLVWGQEPSG ATPTPTATPA PTVTPTPTPT PTSTPTATPT
910 920 930 940 950
ATPTPTPTPS STPVAGGQIK VLYANKETNS TTNTIRPWLK VVNTGSSSID
960 970 980 990 1000
LSRVTIRYWY TVDGDKAQSA ISDWAQIGAS NVTFKFVKLS SSVSGADYYL
1010 1020 1030 1040 1050
EIGFKSGAGQ LQAGKDTGEI QIRFNKSDWS NYNQGNDWSW MQSMTNYGEN
1060 1070 1080 1090 1100
VKVTAYIDGV LVWGQEPSGA TPTPTATPAP TVTPTPTPAP TPTPTPTPTA
1110 1120 1130 1140 1150
TPTPTPTPTP TATPTVTATP TPTPSSTPSV LGEYGQRFMW LWNKIHDPAN
1160 1170 1180 1190 1200
GYFNQDGIPY HSVETLICEA PDYGHLTTSE AFSYYVWLEA VYGKLTGDWS
1210 1220 1230 1240 1250
KFKTAWDTLE KYMIPSAEDQ PMRSYDPNKP ATYAGEWETP DKYPSPLEFN
1260 1270 1280 1290 1300
VPVGKDPLHN ELVSTYGSTL MYGMHWLMDV DNWYGYGKRG DGVSRASFIN
1310 1320 1330 1340 1350
TFQRGPEESV WETVPHPSWE EFKWGGPNGF LDLFIKDQNY SKQWRYTDAP
1360 1370 1380 1390 1400
DADARAIQAT YWAKVWAKEQ GKFNEISSYV AKAAKMGDYL RYAMFDKYFK
1410 1420 1430 1440 1450
PLGCQDKNAA GGTGYDSAHY LLSWYYAWGG ALDGAWSWKI GSSHVHFGYQ
1460 1470 1480 1490 1500
NPMAAWALAN DSDMKPKSPN GASDWAKSLK RQIEFYRWLQ SAEGAIAGGA
1510 1520 1530 1540 1550
TNSWNGRYEK YPAGTATFYG MAYEPNPVYH DPGSNTWFGF QAWSMQRVAE
1560 1570 1580 1590 1600
YYYVTGDKDA GALLEKWVSW VKSVVKLNSD GTFAIPSTLD WSGQPDTWNG
1610 1620 1630 1640 1650
AYTGNSNLHV KVVDYGTDLG ITASLANALL YYSAGTKKYG VFDEGAKNLA
1660 1670 1680 1690 1700
KELLDRMWKL YRDEKGLSAP EKRADYKRFF EQEVYIPAGW IGKMPNGDVI
1710 1720 1730 1740 1750
KSGVKFIDIR SKYKQDPDWP KLEAAYKSGQ APEFRYHRFW AQCDIAIANA

TYEILFGNQ
Length:1,759
Mass (Da):195,134
Last modified:March 24, 2009 - v1
Checksum:i94BB33870F441F32
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001393 Genomic DNA. Translation: ACM60955.1.
RefSeqiWP_015908250.1. NC_012034.1.

Genome annotation databases

EnsemblBacteriaiACM60955; ACM60955; Athe_1867.
KEGGiate:Athe_1867.
PATRICi20900916. VBIAnaThe135187_1952.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001393 Genomic DNA. Translation: ACM60955.1.
RefSeqiWP_015908250.1. NC_012034.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EL8X-ray2.45A1126-1759[»]
4L0GX-ray2.00A1122-1759[»]
4L6XX-ray1.70A1122-1759[»]
4TXTX-ray2.00A1122-1759[»]
ProteinModelPortaliB9MKU7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi521460.Athe_1867.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACM60955; ACM60955; Athe_1867.
KEGGiate:Athe_1867.
PATRICi20900916. VBIAnaThe135187_1952.

Phylogenomic databases

eggNOGiENOG4105CYP. Bacteria.
COG2730. LUCA.
HOGENOMiHOG000269731.
OMAiYRRIIAM.
OrthoDBiEOG6KQ6BP.

Enzyme and pathway databases

BioCyciCBES521460:GH8H-1905-MONOMER.

Family and domain databases

Gene3Di1.50.10.10. 5 hits.
2.60.40.710. 3 hits.
4.10.870.10. 1 hit.
InterProiIPR008928. 6-hairpin_glycosidase-like.
IPR012341. 6hp_glycosidase.
IPR008965. Carb-bd_dom.
IPR001956. CBD_3.
IPR027390. Endoglucanase_F_dom3.
IPR000556. Glyco_hydro_48F.
IPR001701. Glyco_hydro_9.
IPR033126. Glyco_hydro_9_Asp/Glu_AS.
IPR018221. Glyco_hydro_9_His_AS.
[Graphical view]
PfamiPF00942. CBM_3. 3 hits.
PF02011. Glyco_hydro_48. 1 hit.
PF00759. Glyco_hydro_9. 1 hit.
[Graphical view]
PRINTSiPR00844. GLHYDRLASE48.
SMARTiSM01067. CBM_3. 3 hits.
[Graphical view]
SUPFAMiSSF48208. SSF48208. 2 hits.
SSF49384. SSF49384. 3 hits.
PROSITEiPS51172. CBM3. 3 hits.
PS00592. GLYCOSYL_HYDROL_F9_1. 1 hit.
PS00698. GLYCOSYL_HYDROL_F9_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725."
    Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kataeva I., Adams M.W.W.
    Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-1888 / DSM 6725 / Z-1320Imported.
  2. "Structural and biochemical characterization of C. BESCII CelA."
    Alahuhta P.M., Lunin V.V.
    Submitted (APR-2012) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 1126-1759 IN COMPLEX WITH CALCIUM.
  3. "Crystallization and preliminary X-ray analysis of a processive cellobiohydrolase CbCBH48A from Caldicellulosiruptor bescii."
    Jiao A., Bai A., Yan F., Geng W.
    Submitted (JUN-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1122-1759.
  4. "Crystallization and preliminary X-ray analysis of a processive cellobiohydrolase CbCBH48A from Caldicellulosiruptor bescii."
    An J., Feng Y., Bai A.
    Submitted (JUL-2014) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1122-1759.

Entry informationi

Entry nameiB9MKU7_CALBD
AccessioniPrimary (citable) accession number: B9MKU7
Entry historyi
Integrated into UniProtKB/TrEMBL: March 24, 2009
Last sequence update: March 24, 2009
Last modified: March 16, 2016
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.