Unreviewed, UniProtKB/TrEMBL Q700S9 (Q700S9_PENSQ)

Names and origin

Protein names

Recommended name:
    Beta-galactosidase RuleBase RU000675V2
    EC=3.2.1.23 RuleBase RU000675V2

Gene names

Name:

lac EMBL CAF32457.1

Organism

Penicillium sp. EMBL CAF32457.1

Taxonomic identifier

5081 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium

Protein attributes

Sequence length	1011 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. RuleBase RU000675V2
Sequence similarities	Belongs to the glycosyl hydrolase 35 family.

Ontologies

Keywords
Domain	Signal EMBL CAF32457.1
Molecular function	Glycosidase RuleBase RU000675V2 Spearmint SPM001944 EMBL CAF32457.1 Hydrolase
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactosidase 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
	Signal peptide	1 – 39	39	EMBL CAF32457.1
	Chain	40 – 1011	972	beta-galactosidase EMBL CAF32457.1		PRO_5000072460

Sequences

	Sequence		Length	Mass (Da)
	Q700S9-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: A8A5BD48354F791A	FASTA	1,011	109,750
	10 20 30 40 50 60 MKLLSSWVVA ALAAQAAGAA ISHKLDGFTI REHADPAKRA LLQKYVTWDE HSIFVNGERL 70 80 90 100 110 120 MIFSGEVHPY RLPVASLYID IFEKVKALGF NCVSFYVDWA LLEGNPGHYS AEGIFDLQPF 130 140 150 160 170 180 FDAAKEAGIY LLARPGPYIN AEVSGGGFPG WLQRVDGILR TSDEAYLKAT DNYASNIAAT 190 200 210 220 230 240 IAKAQITNGG PIILYQPENE YSGACCGYNG FPDGSYMQYI EDHARDAGIV VPFISNDAWA 250 260 270 280 290 300 AGHNAPGTGA GAVDIYGHDS YPLGFDCANP STWPSGNLPT YFHTSHEQQS PSTPYSLVEF 310 320 330 340 350 360 QGGAFDPWGG VGFAKCAALL NHEFERVFYK NDFSFGVAFL NLYMIFGGTN WGNLGHPGGY 370 380 390 400 410 420 TSYDYGSAIS ESRNITREKY SELKLLGNFA KVSPGYLVAN PGDLSTSTYT NTADLTVTPL 430 440 450 460 470 480 LGSNSSASSF FVIRHSDYSS QASVEYKLTV PTSAGNLTIP QLGGSLTLSG RDSKIHVTDY 490 500 510 520 530 540 DVAGTNILYS TAEVFTWKKF NNEKVLVLYG GPGEHHEFAV SGASSSSVVE GSSSGISSKK 550 560 570 580 590 600 VGKALVVAWD VSTARRIVQV GSLKVFLLDR NSAYNYWVPQ VPTKGTAPGY SNQETTASSI 610 620 630 640 650 660 IVKAGYLVRS AYLDGNDLHI QADFNATTPI EVVGAPSGAK NLVINGKKTQ TKVDKNGIWS 670 680 690 700 710 720 ASVAYTAPKV QLPSLKSLKW KSVDTLPEAK NTYDDSAWTS ADHAYTNNSA HSLQTPTSLF 730 740 750 760 770 780 ASDYGYHTGA LLFRGHFTAN GKEKTFFVQT KGGTAYGHSI WINETYVGSW AGTSINDNNN 790 800 810 820 830 840 ATYTLPTLQS GKNYVITVVI DNMGLDEDWT IGSEDMKNPR GIIQYSLSGQ EASAISWKLT 850 860 870 880 890 900 GNLGGENYRD TVRGPLNEGG LYAERQGFHQ PQPPTQKWDS SSPFTGLTKP GIRFYSTSFD 910 920 930 940 950 960 LDLPSGYDIP LYFNFGNSTS TPAAYRVQLY VNGYQYGKYV NNIGPQTSFP VPEGILNYHG 970 980 990 1000 1010 TNWLALSLWA QEDNGAKLDS FELINTTPVL TSLGEVKSVN QPKYQARKGA Y

References

[1]	"Crystal structure of beta-galactosidase from Penicillium sp. and its complex with galactose." Rojas A.L., Nagem R.A.P., Neustroev K.N., Golubev A.M., Arand M., Adamska M., Eneyskaya E.V., Kulminskaya A.A., Polikarpov I. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Crystal structures of beta-galactosidase from Penicillium sp. and its complex with galactose." Rojas A.L., Nagem R.A., Neustroev K.N., Arand M., Adamska M., Eneyskaya E.V., Kulminskaya A.A., Garratt R.C., Golubev A.M., Polikarpov I. J. Mol. Biol. 343:1281-1292(2004) [PubMed: 15491613] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 41-1011.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ629057 Genomic DNA. Translation: CAF32457.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TG7	X-ray	1.90	A	41-1011	[»]
1XC6	X-ray	2.10	A	41-1011	[»]

ModBase

Search...

Protein family/group databases

CAZy

GH35. Glycoside Hydrolase Family 35.

Family and domain databases

InterPro

IPR018954. Beta-galactosidase_domain-2.
IPR019801. Glyco_hydro_35_CS.
IPR017853. Glyco_hydro_catalytic_core.
IPR013781. Glyco_hydro_sg_catalytic.
IPR001944. Glycoside_Hdrlase_35.
[Graphical view]

Gene3D

G3DSA:2.102.20.10. Beta-galactosidase_domain-2. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

PANTHER

PTHR23421. Glyco_hydro_35. 1 hit.

Pfam

PF10435. BetaGal_dom2. 1 hit.
PF01301. Glyco_hydro_35. 1 hit.
[Graphical view]

PRINTS

PR00742. GLHYDRLASE35.

PROSITE

PS01182. GLYCOSYL_HYDROL_F35. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q700S9_PENSQ

Accession

Primary (citable) accession number: Q700S9

Entry history

Integrated into UniProtKB/TrEMBL:	July 5, 2004
Last sequence update:	July 5, 2004
Last modified:	November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)