S-layer associated multidomain endoglucanase - Caldanaerobius polysaccharolyticus

Preferred order of sections

Names and origin

Protein names

Submitted name:
S-layer associated multidomain endoglucanase EMBL AAD09354.1

Gene names

Name:

celA EMBL AAD09354.1

Organism

Caldanaerobius polysaccharolyticus EMBL AAD09354.1

Taxonomic identifier

44256 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Thermoanaerobacterales › Thermoanaerobacteriaceae › Caldanaerobius

Protein attributes

Sequence length	1097 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 2ZEW PDB 2ZEX PDB 2ZEY PDB 2ZEZ PDB 3OEA PDB 3OEB Metal-binding PDB 2ZEW PDB 2ZEX PDB 2ZEY PDB 2ZEZ PDB 3OEA PDB 3OEB
Technical term	3D-structure PDB 2ZEW PDB 2ZEX PDB 2ZEY PDB 2ZEZ PDB 3OEA PDB 3OEB
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Region

632 – 633

2

Beta-D-mannose binding PDB 2ZEY PDB 3OEB

Sites

Metal binding

621

1

Calcium 1; via carbonyl oxygen PDB 2ZEW PDB 2ZEX PDB 2ZEY PDB 3OEA PDB 3OEB

Metal binding

623

1

Calcium 1 PDB 2ZEW PDB 2ZEX PDB 2ZEY PDB 3OEA PDB 3OEB

Metal binding

645

1

Calcium 1; via carbonyl oxygen PDB 2ZEW PDB 2ZEX PDB 2ZEY PDB 3OEA PDB 3OEB

Metal binding

648

1

Calcium 1; via carbonyl oxygen PDB 2ZEW PDB 2ZEX PDB 2ZEY PDB 3OEA PDB 3OEB

Metal binding

749

1

Calcium 1 PDB 2ZEW PDB 2ZEX PDB 2ZEY PDB 3OEA PDB 3OEB

Metal binding

764

1

Calcium 2; via carbonyl oxygen PDB 2ZEZ

Metal binding

766

1

Calcium 2 PDB 2ZEZ

Metal binding

788

1

Calcium 2; via carbonyl oxygen PDB 2ZEZ

Metal binding

791

1

Calcium 2; via carbonyl oxygen PDB 2ZEZ

Metal binding

892

1

Calcium 2 PDB 2ZEZ

Binding site

689

1

Beta-D-mannose PDB 3OEB

Binding site

693

1

Beta-D-mannose PDB 2ZEY PDB 3OEB

Binding site

705

1

Beta-D-mannose PDB 2ZEY PDB 3OEB

Binding site

709

1

Beta-D-mannose PDB 2ZEY

Binding site

709

1

Glucose PDB 3OEA

Binding site

709

1

Mannose PDB 3OEB

Binding site

733

1

Beta-D-mannose PDB 2ZEY

Binding site

737

1

Beta-D-mannose PDB 2ZEY PDB 3OEB

Sequences

Sequence

Length

Mass (Da)

Tools

Q9ZA17 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C41C6EB92C0494B9
Show »

FASTA

1,097

119,763

        10         20         30         40         50         60 
MKKVLSKLMV FVMVLTVALG NGVFIGDKQA KAAGTSGDGR FHVVGNKIVD PDGNDFVIKG 

        70         80         90        100        110        120 
VNIQGYRSWE KRSVLQDVHL IADVWKFNTV RLNCFIGQNN WGEGTGANND IDAIIKAFTA 

       130        140        150        160        170        180 
KKVVVEIDLH DTTGYPPLSN PPPAPGQPSL DQAIAWFKEL AAKYKDNPYV WFNTMNEPGS 

       190        200        210        220        230        240 
STAPLDPQWK VANEEIIKAI RSTGADNIIV VDGWSYANEG IEQNTPTVDE KRSAVLTYGQ 

       250        260        270        280        290        300 
DLLNADSAKN TIFAFHNYNE GDIQKKVEDY IDRANAKGLY VFMEEYGKDY SDAAKEGVKS 

       310        320        330        340        350        360 
GLQAVMNKGA GRIYWNWDGY DLYDLTSGTG RGSGWEINKT DGSKPTNLSW VGDKIWDDNH 

       370        380        390        400        410        420 
GITPTFDDQN PKVDLALERL IANNNGFKAG DKVQFTTFLR NSGDLPIGKD SKVVVKFYVD 

       430        440        450        460        470        480 
GVQLGDPVEI SGGIAVGQRI PVTSPELTVS KTDFTVKAVI DSSSTYADGA EDAVIENNWI 

       490        500        510        520        530        540 
EAAFNSTAPS SGYELVVTGI KITPDTVKER DYVQAQVTVA NQGPEATPVT NIIGWFYVNG 

       550        560        570        580        590        600 
YYYTLDDAAK SCAEQDNVTL KPGESITLST KVKYRAAAPC NFSFVLENLY ADDQNQSNNS 

       610        620        630        640        650        660 
ITVNVPVKMG EGGVNMVSNP GFEDGLDSWQ DWQQDMSAVP EAAHNGALGL KIGGGKAAGG 

       670        680        690        700        710        720 
GQDIPLKPNT TYILGAWAKF DSKPAGTFDV VVQYHLKDAN NTYVQHILNF NETDWTYKQL 

       730        740        750        760        770        780 
LFTTPDVFGS TPQLALWKGD TSKANLYVDD VYLVEVSNLI VNGTAENGMD GWPDWGYPVS 

       790        800        810        820        830        840 
AVPEAAYGGT KGFKLSGGKQ AGMGQKVALK PNTTYILGAW GKFTAKPGTY CDVIVQYHLK 

       850        860        870        880        890        900 
DANNTYVQNI LRFTETDWTY KQVVFTTPDA FGSDPEFVLW KDDASNADFY ADNITLVEVP 

       910        920        930        940        950        960 
SSMVNKGSIA PKFTDISSSW AKNEIQVLAS KNIISGYPDG TFKPDKRITR AEFVSMLVKA 

       970        980        990       1000       1010       1020 
LGIKQSIPDV PTFSDVNKGD WYYGLVEAAK STGIASGYGK QFKPDMQITR QEMMVMVVNA 

      1030       1040       1050       1060       1070       1080 
LRVNKVEKFV SKGDVSVLGK FKDGGKVQNW AKDAMAIGVS NGLIKGTGDE YLSPDGRATR 

      1090 
AQAAAVIYRM LLQLGRI

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References

[1]	"Molecular cloning, sequencing, and expression of a novel multidomain mannanase gene from Thermoanaerobacterium polysaccharolyticum." Cann I.K., Kocherginskaya S., King M.R., White B.A., Mackie R.I. J. Bacteriol. 181:1643-1651(1999) [PubMed: 10049399] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: KM-THCJ EMBL AAD09354.1.
[2]	Cann I.K.O., White B.A., Mackie R.I. Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: KM-THCJ EMBL AAD09354.1.
[3]	"Molecular basis for the selectivity and specificity of ligand recognition by the family 16 carbohydrate-binding modules from Thermoanaerobacterium polysaccharolyticum ManA." Bae B., Ohene-Adjei S., Kocherginskaya S., Mackie R.I., Spies M.A., Cann I.K., Nair S.K. J. Biol. Chem. 283:12415-12425(2008) [PubMed: 18025086] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 614-756 IN COMPLEX WITH BETA-D-MANNOSE AND CALCIUM.
[4]	"Mutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules." Su X., Agarwal V., Dodd D., Bae B., Mackie R.I., Nair S.K., Cann I.K. J. Biol. Chem. 285:34665-34676(2010) [PubMed: 20739280] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 614-756 IN COMPLEX WITH BETA-D-MANNOSE; CALCIUM; GLUCOSE AND MANNOSE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U82255 Genomic DNA. Translation: AAD09354.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ZEW	X-ray	1.40	A/B	614-756	[»]
2ZEX	X-ray	1.20	A/B	614-756	[»]
2ZEY	X-ray	2.20	A/B	614-756	[»]
2ZEZ	X-ray	1.90	A/B/C/D	756-899	[»]
3OEA	X-ray	1.35	A/B	614-756	[»]
3OEB	X-ray	1.55	A	614-756	[»]

ProteinModelPortal

Q9ZA17.

SMR

Q9ZA17. Positions 614-898.

ModBase

Search...

Protein family/group databases

CAZy

CBM16. Carbohydrate-Binding Module Family 16.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. S-layer_homology_dom.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF02018. CBM_4_9. 2 hits.
PF00150. Cellulase. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]

SUPFAM

SSF49785. Gal_bind_like. 2 hits.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS51272. SLH. 3 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9ZA17_9THEO

Accession

Primary (citable) accession number: Q9ZA17

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 1999
Last sequence update:	May 1, 1999
Last modified:	October 19, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)