Laminarinase - Thermotoga maritima

Preferred order of sections

Names and origin

Protein names

Submitted name:
Laminarinase EMBL AAD35118.1

Gene names

Ordered Locus Names:

TM_0024

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	642 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Calcium PDB 1GUI Metal-binding PDB 1GUI
Technical term	3D-structure PDB 1GUI Complete proteome Reference proteome
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

Sites

Metal binding

493

1

Calcium; via carbonyl oxygen PDB 1GUI

Metal binding

532

1

Calcium; via carbonyl oxygen PDB 1GUI

Metal binding

635

1

Calcium PDB 1GUI

Sequences

Sequence

Length

Mass (Da)

Tools

Q9WXN1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 6431C9825597BF7E
Show »

FASTA

642

72,540

        10         20         30         40         50         60 
MMSRLVFALL LFPVFILAQN ILGNASFDEP ILIAGVDIDP PAEDGSIDTG GNWVFFTNSN 

        70         80         90        100        110        120 
GEGTARVENG VLVVEITNGG DHTWSVQIIQ APIRVEKLHK YRVSFRAKAS SQKNIGVKIG 

       130        140        150        160        170        180 
GTAGRGWTAY NPGTDESGGM VFELGTDWQK YEFEFVMRQE TDENARFEFQ LGRYTGTVWI 

       190        200        210        220        230        240 
DDVVMEDIGV LEVSGEENEI YTEEDEDKVE DWQLVWSQEF DDGVIDPNIW NFEIGNGHAK 

       250        260        270        280        290        300 
GIPGWGNGEL EYYTDENAFV ENGCLVIEAR KEQVSDEYGT YDYTSARMTT EGKFEIKYGK 

       310        320        330        340        350        360 
IEIRAKLPKG KGIWPALWML GNNIGEVGWP TCGEIDIMEM LGHDTRTVYG TAHGPGYSGG 

       370        380        390        400        410        420 
ASIGVAYHLP EGVPDFSEDF HIFSIEWDED EVEWYVDGQL YHVLSKDELA ELGLEWVFDH 

       430        440        450        460        470        480 
PFFLILNVAV GGYWPGYPDE TTQFPQRMYI DYIRVYKDMN PETITGEVDD CEYEQAQQQA 

       490        500        510        520        530        540 
GPEVTYEQIN NGTFDEPIVN DQANNPDEWF IWQAGDYGIS GARVSDYGVR DGYAYITIAD 

       550        560        570        580        590        600 
PGTDTWHIQF NQWIGLYRGK TYTISFKAKA DTPRPINVKI LQNHDPWTNY FAQTVNLTAD 

       610        620        630        640 
WQTFTFTYTH PDDADEVVQI SFELGEGTAT TIYFDDVTVS PQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima." Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules." Boraston A.B., Nurizzo D., Notenboom V., Ducros V., Rose D.R., Kilburn D.G., Davies G.J. J. Mol. Biol. 319:1143-1156(2002) [PubMed: 12079353] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 489-642 IN COMPLEX WITH CALCIUM.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000512 Genomic DNA. Translation: AAD35118.1.

PIR

B72428.

RefSeq

NP_227840.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GUI	X-ray	1.90	A	489-642	[»]
3AZX	X-ray	1.80	A/B	204-466	[»]
3AZY	X-ray	1.65	A/B/C/D	204-466	[»]
3AZZ	X-ray	1.81	A/B/C/D	204-466	[»]
3B00	X-ray	1.74	A/B/C/D	204-466	[»]
3B01	X-ray	1.87	A/B/C/D	204-466	[»]

ProteinModelPortal

Q9WXN1.

SMR

Q9WXN1. Positions 489-642.

ModBase

Search...

Protein family/group databases

CAZy

CBM4. Carbohydrate-Binding Module Family 4.
GH16. Glycoside Hydrolase Family 16.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

896840.

GenomeReviews

Gene locus TM_0024 in contig AE000512_GR.

KEGG

tma:TM0024.

NMPDR

fig|243274.1.peg.24.

PATRIC

23934888. VBITheMar51294_0022.

TIGR

TM_0024.

Phylogenomic databases

HOGENOM

HBG465560.

OMA

ARFEFQL.

PhylomeDB

Q9WXN1.

ProtClustDB

CLSK794849.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_0024-MONOMER.

Family and domain databases

InterPro

IPR003305. CenC_carb-bd.
IPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR008979. Galactose-bd-like.
IPR000757. Glyco_hydro_16.
[Graphical view]

Gene3D

G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.

Pfam

PF02018. CBM_4_9. 2 hits.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.
SSF49785. Gal_bind_like. 2 hits.

ProtoNet

Search...

Entry information

Entry name

Q9WXN1_THEMA

Accession

Primary (citable) accession number: Q9WXN1

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1999
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)