Q9XCV5 (Q9XCV5_CELFI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Man26A EMBL AAD42774.1

Gene names

Name:

man26A EMBL AAD42774.1

Organism

Cellulomonas fimi EMBL AAD42774.1

Taxonomic identifier

1708 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

Protein attributes

Sequence length	1010 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Magnesium PDB 2X2Y Metal-binding PDB 2X2Y
Technical term	3D-structure PDB 2BVT PDB 2X2Y PDB 2BVY
Gene Ontology (GO)
Biological process	cellulose catabolic process Inferred from electronic annotation. Source: InterPro substituted mannan metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	cellulase activity Inferred from electronic annotation. Source: InterPro mannan endo-1,4-beta-mannosidase activity 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	397	1	Magnesium; via carbonyl oxygen PDB 2X2Y
	Metal binding	399	1	Magnesium; via carbonyl oxygen PDB 2X2Y
	Metal binding	402	1	Magnesium PDB 2X2Y
	Binding site	127	1	Beta-D-mannose; via carbonyl oxygen PDB 2BVT
	Binding site	372	1	Beta-D-mannose PDB 2BVT
	Binding site	379	1	Beta-D-mannose PDB 2BVT

Sequences

	Sequence		Length	Mass (Da)
	Q9XCV5 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: C7DBC630F4CE58C8	FASTA	1,010	107,110
	10 20 30 40 50 60 MTNRSRPRGR TAGHVLAATA AALALTGLSA LPAQSAPAPA APVAGALPTA PADETIAIVD 70 80 90 100 110 120 ADATAETRSL LSYLDGVRGE GILFGHQHTT SFGLTTGPTD GTTSDVKNVT GDFPAVFGWD 130 140 150 160 170 180 TLIIEGNERP GLAENTRDEN IALFADYIRK ADAIGGVNTV SAHVENFVTG GSFYDTSGDT 190 200 210 220 230 240 LRAVLPGGSH HAELVAYLDD IAELADASRR DDGTLIPIVF RPWHENAGSW FWWGAAYGSP 250 260 270 280 290 300 GEYQELYRFT VEYLRDVKGV SNFLYAWGPG GGFGGNRDVY LRTYPGDAFV DVLGLDTYDS 310 320 330 340 350 360 TGSDAFLAGL VADLRMIAEI ADEKGKVSAF TEFGVSGGVG TNGSSPAQWF TKVLAAIKAD 370 380 390 400 410 420 PVASRNAYME TWANFDAGQH FVPVPGDALL EDFQAYAADP FTLFASEVTG AFDRTVAAAP 430 440 450 460 470 480 AQPVVHIASP ADGARVASAP TTVRVRVGGT DVQSVTVEVA QGGTVVDTLD LAYDGALWWT 490 500 510 520 530 540 APWSPTSAQL DNSTYTVTAT ATTAAGTLDV TNEVVLGPRP TFPAGVVDDF EGYGDDTALR 550 560 570 580 590 600 AEYVTYGANT ISLETGSVGG GAKALRLDYD FATQTYTGVG KQLSGDWSDF NELAIWVDPD 610 620 630 640 650 660 GSNNRMVLQL NAGGVAYEAY PSLAGDEPQL VTIPFVDWRP APWDTAHADR RMSDDDLRAL 670 680 690 700 710 720 TSFNVYVNSA EGGAASGSLV VDDIAAHPGV EPPPLFSDVP KGHPYETEIL WLHAQGLDDG 730 740 750 760 770 780 YDDGTFRPAR QVKRQDVARL LHAYEKAVFT PPTTPSFLDV RRSHPAYTAI EWLVAEGLVD 790 800 810 820 830 840 DGRVFLPSAP LDRATAAELL WRLAGSPEPE GTEAFRDVPT WHRYRTAITW ATEVGVVEPV 850 860 870 880 890 900 SASTFGVLKA VQRQELARYL YRFDALPSPL EPVVLSDFAD GAQGWGPLDA GPGSATASGG 910 920 930 940 950 960 TLTIEAAAPD GGWFSFTPSV ADWTGRTALA LDVVSTTGFD TKAALQVGST WQWCETAQAG 970 980 990 1000 1010 WVSGPRTGDD ALVLDLTTLY AGCGAQLADV KRVNLYLNAG THVIDDVELR

References

[1]	"Mannan-degrading enzymes from Cellulomonas fimi." Stoll D., Stalbrand H., Warren R.A. Appl. Environ. Microbiol. 65:2598-2605(1999) [PubMed: 10347049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 484 EMBL AAD42774.1.
[2]	"Rational engineering of mannosyl binding in the distal glycone subsites of Cellulomonas fimi endo-beta-1,4-mannanase: mannosyl binding promoted at subsite -2 and demoted at subsite -3." Hekmat O., Lo Leggio L., Rosengren A., Kamarauskaite J., Kolenova K., Stalbrand H. Biochemistry 49:4884-4896(2010) [PubMed: 20426480] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 52-514 IN COMPLEX WITH MAGNESIUM.
[3]	"The structure and characterization of a modular endo-beta-1,4-mannanase from Cellulomonas fimi." Le Nours J., Anderson L., Stoll D., Stalbrand H., Lo Leggio L. Biochemistry 44:12700-12708(2005) [PubMed: 16171384] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 52-514 IN COMPLEX WITH BETA-D-MANNOSE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF126471 Genomic DNA. Translation: AAD42774.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BVT	X-ray	2.90	A/B	52-514	[»]
2BVY	X-ray	2.25	A	52-514	[»]
2X2Y	X-ray	2.35	A/B	52-514	[»]

ProteinModelPortal

Q9XCV5.

SMR

Q9XCV5. Positions 55-514.

ModBase

Search...

Protein family/group databases

CAZy

CBM23. Carbohydrate-Binding Module Family 23.
GH26. Glycoside Hydrolase Family 26.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR005087. CBM_fam11.
IPR022790. EndoGluc_H/Glyco_hydro_26.
IPR008979. Galactose-bd-like.
IPR000805. Glyco_hydro_26.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
IPR014756. Ig_E-set.
IPR001119. S-layer_homology_dom.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF03425. CBM_11. 1 hit.
PF02156. Glyco_hydro_26. 1 hit.
PF00395. SLH. 1 hit.
[Graphical view]

PRINTS

PR00739. GLHYDRLASE26.

SUPFAM

SSF49785. Gal_bind_like. 1 hit.
SSF51445. Glyco_hydro_cat. 1 hit.
SSF81296. Ig_E-set. 1 hit.

PROSITE

PS51272. SLH. 3 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q9XCV5_CELFI

Accession

Primary (citable) accession number: Q9XCV5

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1999
Last sequence update:	November 1, 1999
Last modified:	July 27, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)