Alpha-glucuronidase - Cellvibrio japonicus

Preferred order of sections

Names and origin

Protein names

Submitted name:
Alpha-glucuronidase EMBL AAL57752.1

Gene names

Name:

glcA67A EMBL AAL57752.1

Organism

Cellvibrio japonicus EMBL AAL57752.1

Taxonomic identifier

155077 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Cellvibrio

Protein attributes

Sequence length	732 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Technical term	3D-structure PDB 1GQI PDB 1GQJ PDB 1GQL PDB 1GQK PDB 1H41
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-glucuronidase activity Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

173

1

Cobalt PDB 1H41

Metal binding

174

1

Cobalt; via tele nitrogen PDB 1H41

Metal binding

458

1

Cobalt; via pros nitrogen PDB 1H41

Sequences

Sequence

Length

Mass (Da)

Tools

Q8VP74 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: E3219C0AB50E7685
Show »

FASTA

732

83,021

        10         20         30         40         50         60 
MSTFARLFLC LVFFASLQPA MAQTEDGYDM WLRYQPIADQ TLLKTYQKQI RHLHVAGDSP 

        70         80         90        100        110        120 
TINAAAAELQ RGLSGLLNKP IVARDEKLKD YSLVIGTPDN SPLIASLNLG ERLQALGAEG 

       130        140        150        160        170        180 
YLLEQTRINK RHVVIVAANS DVGVLYGSFH LLRLIQTQHA LEKLSLSSAP RLQHRVVNHW 

       190        200        210        220        230        240 
DNLNRVVERG YAGLSLWDWG SLPNYLAPRY TDYARINASL GINGTVINNV NADPRVLSDQ 

       250        260        270        280        290        300 
FLQKIAALAD AFRPYGIKMY LSINFNSPRA FGDVDTADPL DPRVQQWWKT RAQKIYSYIP 

       310        320        330        340        350        360 
DFGGFLVKAD SEGQPGPQGY GRDHAEGANM LAAALKPFGG VVFWRAFVYH PDIEDRFRGA 

       370        380        390        400        410        420 
YDEFMPLDGK FADNVILQIK NGPIDFQPRE PFSALFAGMS RTNMMMEFQI TQEYFGFATH 

       430        440        450        460        470        480 
LAYQGPLFEE SLKTETHARG EGSTIGNILE GKVFKTRHTG MAGVINPGTD RNWTGHPFVQ 

       490        500        510        520        530        540 
SSWYAFGRMA WDHQISAATA ADEWLRMTFS NQPAFIEPVK QMMLVSREAG VNYRSPLGLT 

       550        560        570        580        590        600 
HLYSQGDHYG PAPWTDDLPR ADWTAVYYHR ASKTGIGFNR TKTGSNALAQ YPEPIAKAWG 

       610        620        630        640        650        660 
DLNSVPEDLI LWFHHLSWDH RMQSGRNLWQ ELVHKYYQGV EQVRAMQRTW DQQEAYVDAA 

       670        680        690        700        710        720 
RFAQVKALLQ VQEREAVRWR NSCVLYFQSV AGRPIPANYE QPEHDLEYYK MLARTTYVPE 

       730 
PWHPASSSRV LK

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References

[1]	"The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan." Nagy T., Emami K., Fontes C.M., Ferreira L.M., Humphry D.R., Gilbert H.J. J. Bacteriol. 184:4925-4929(2002) [PubMed: 12169619] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants." Nagy T., Nurizzo D., Davies G.J., Biely P., Lakey J.H., Bolam D.N., Gilbert H.J. J. Biol. Chem. 278:20286-20292(2003) [PubMed: 12654910] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 25-732.
[3]	"The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A." Nurizzo D., Nagy T., Gilbert H.J., Davies G.J. Structure 10:547-556(2002) [PubMed: 11937059] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 25-732.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY065638 Genomic DNA. Translation: AAL57752.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GQI	X-ray	1.48	A/B	25-732	[»]
1GQJ	X-ray	1.90	A/B	25-732	[»]
1GQK	X-ray	1.90	A/B	25-732	[»]
1GQL	X-ray	1.67	A/B	25-732	[»]
1H41	X-ray	1.50	A/B	25-732	[»]

ProteinModelPortal

Q8VP74.

SMR

Q8VP74. Positions 25-732.

ModBase

Search...

Protein family/group databases

CAZy

GH67. Glycoside Hydrolase Family 67.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.2.1.139. 191848.

Family and domain databases

InterPro

IPR011395. Glyco_hydro_67_aGlcAse.
IPR005154. Glyco_hydro_67_aGlcAse_N.
IPR011099. Glyco_hydro_67_C.
IPR011100. Glyco_hydro_67_M.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.90.1330.10. Glyco_hydro_67_C. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF07477. Glyco_hydro_67C. 1 hit.
PF07488. Glyco_hydro_67M. 1 hit.
PF03648. Glyco_hydro_67N. 1 hit.
[Graphical view]

PIRSF

PIRSF029900. Alpha-glucuronds. 1 hit.

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q8VP74_9GAMM

Accession

Primary (citable) accession number: Q8VP74

Entry history

Integrated into UniProtKB/TrEMBL:	March 1, 2002
Last sequence update:	March 1, 2002
Last modified:	October 19, 2011
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)