P96105 (AGUA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-glucuronidase
EC=3.2.1.139

Alternative name(s):
Alpha-glucosiduronase

Gene names

Name:	aguA
Ordered Locus Names:	TM_0055

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	674 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Releases 4-O-methylglucuronic acid from substituted xylo-oligosaccharides.
Catalytic activity	An alpha-D-glucuronoside + H2O = an alcohol + D-glucuronate.
Subunit structure	Homooligomer.
Sequence similarities	Belongs to the glycosyl hydrolase 67 family.
Biophysicochemical properties	pH dependence: Optimum pH is 6.3. Temperature dependence: Optimum temperature is 85 degrees Celsius.

Ontologies

Keywords
Biological process	Xylan degradation
Molecular function	Glycosidase Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-glucuronidase activity Inferred from electronic annotation. Source: EC cation binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 674	674	Alpha-glucuronidase		PRO_0000057716

Sequences

	Sequence		Length	Mass (Da)
	P96105 [UniParc]. Last modified July 1, 1997. Version 2. Checksum: 350F1CBEDE452761	FASTA	674	78,629
	10 20 30 40 50 60 MDYRMCWLEY RGLPADVAGK LKDWFSSVSI LEPGSSVLKD EIRRFSERSI GITPRFYSRP 70 80 90 100 110 120 LKKEKYIMVG RLESLPIKLD VNLGEEGFML RTIEWNGSKI LLVTGETKKA LVYGIFDLMK 130 140 150 160 170 180 RIRLGEDIEK MNVLAKPKAK FRMLNHWDNL DGTIERGYAG NSIFFKDNRI IINQRTKDYA 190 200 210 220 230 240 RLLASIGING VVINNVNVKK REVYLIDSIY LKKLKKLADI FREYGIKIYL SINFASPVYL 250 260 270 280 290 300 GGLDTADPLD ERVARWWREK ARGIYDYIPD FGGFLVKADS EFNPGPHMFG RTHAEGANML 310 320 330 340 350 360 ARALAPFGGV VIWRAFVYNC LQDWRDYKTD RAKAAYDNFK PLDGQFDDNV IIQIKYGPMD 370 380 390 400 410 420 FQVREPVNPL FGGMEKTNQI LELQITQEYT GQQIHLCFLG TLWKEILEFD TFAKGEGSYV 430 440 450 460 470 480 KRIVDGTLFD RENNGFAGVS NVGDSVNWTG HDLAQANLYA FGRLAWNPDE EIERIVEEWI 490 500 510 520 530 540 KLTFGDDEKV LENVSYMLMK SHRTYEKYTT PFGLGWMVNP GHHYGPNPEG YEYSKWGTYH 550 560 570 580 590 600 RANWEAIGVD RTSRGTGYTL QYHSPWKEIY DDINTCPEDL LLFFHRVRYD HRLKSGKTLL 610 620 630 640 650 660 QTMYDLHFEG VEEVEEFIKK WEELKDRVSP DIFERVKERL HMQLEHAKEW RDVINTYFYR 670 RTGIPDEKGR KIYP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and analysis of a gene encoding alpha-glucuronidase, an enzyme with a novel primary structure involved in the breakdown of xylan." Ruile P., Winterhalter C., Liebl W. Mol. Microbiol. 23:267-279(1997) [PubMed: 9044261] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]	"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. , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y09510 Genomic DNA. Translation: CAA70702.1. AE000512 Genomic DNA. Translation: AAD35149.1.
PIR	H72423.
RefSeq	NP_227871.1. NC_000853.1.
3D structure databases
ProteinModelPortal	P96105.
SMR	P96105. Positions 3-674.
ModBase	Search...
Protein family/group databases
CAZy	GH67. Glycoside Hydrolase Family 67.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	896879.
GenomeReviews	Gene locus TM_0055 in contig AE000512_GR.
KEGG	tma:TM0055.
NMPDR	fig|243274.1.peg.55.
PATRIC	23934950. VBITheMar51294_0053.
TIGR	TM_0055.
Phylogenomic databases
HOGENOM	HBG293196.
OMA	HAEGANM.
ProtClustDB	CLSK872917.
Enzyme and pathway databases
BioCyc	TMAR243274:TM_0055-MONOMER.
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.
KO	K01235.
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

AGUA_THEMA

Accession

Primary (citable) accession number: P96105

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 81 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program