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Protein
Submitted name:

Beta-galactosidase

Gene

lacZ

Organism
Arthrobacter sp. C2-2
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.SAAS annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi525 – 5251Magnesium; via carbonyl oxygenCombined sources
Metal bindingi527 – 5271Magnesium; via carbonyl oxygenCombined sources
Metal bindingi529 – 5291Magnesium; via carbonyl oxygenCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseSAAS annotationImported, Hydrolase

Keywords - Ligandi

MagnesiumCombined sources, Metal-bindingCombined sources

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Submitted name:
Beta-galactosidaseImported (EC:3.2.1.23Imported)
Gene namesi
Name:lacZImported
OrganismiArthrobacter sp. C2-2Imported
Taxonomic identifieri192168 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeArthrobacter

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YQ2X-ray1.90A/B/C/D/E/F1-1023[»]
ProteinModelPortaliQ8KRF6.
SMRiQ8KRF6. Positions 4-1023.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8KRF6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini738 – 1021284Bgal_small_NInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.SAAS annotation

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR004199. B-gal_small/dom_5.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. GH-type_carb-bd.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR006103. Glyco_hydro_2_cat.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR032312. LacZ_4.
[Graphical view]
PfamiPF02929. Bgal_small_N. 1 hit.
PF16353. DUF4981. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSiPR00132. GLHYDRLASE2.
SMARTiSM01038. Bgal_small_N. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8KRF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTADVSYLT DQGPGSGRRV PARSWLHSDA PALSLNGDWR FRLLPAAPGT
60 70 80 90 100
AGAGSVLPSG ETVEGVAAES YDDAAWDTLP VPSHWVMGQD GKYGRPIYTN
110 120 130 140 150
VQYPFPIDPP HVPDANPTGD FRRRFDVPAQ WFESTTAALT LRFDGVESRY
160 170 180 190 200
KVWVNGQEIG VGSGSRLAQE FDVSDALRAG SNLLVVRVHQ WSAASYLEDQ
210 220 230 240 250
DQWWLPGIFR DVTLQARPAG GITDAWLRTG WSARSGAGTG TIDPEITADA
260 270 280 290 300
TAFPVTLSVP ELGVNVTWKS AEEVAPLALE NVEPWSAEVP RLYEASVSSA
310 320 330 340 350
AESISVRLGF RTVRIVGDQF LVNGRRVVFH GVNRHETHPD RGRVFDEAGA
360 370 380 390 400
REDLALMKRF NVNAIRTSHY PPHPRLLDLA DEMGFWVILE CDLETHGFEA
410 420 430 440 450
GGWVENPSDV PAWRDALVDR MERTVERDKN HPSIVMWSLG NESGTGSNLA
460 470 480 490 500
AMAAWAHARD SSRPVHYEGD YTGAYTDVYS RMYSSIPETD SIGRNDSHAL
510 520 530 540 550
LLGCDSAESA RQRTKPFILC EYVHAMGNGP GAMDQYEALV DKYPRLHGGF
560 570 580 590 600
VWEWRDHGIR TRTAEGMEFF AYGGDFGEVV HDSNFVMDGM VLSDSTPTPG
610 620 630 640 650
LYEFKQIVSP IRLGLSLPAG GKPTLAVANL RHTADASDVV LRWRVEHDGA
660 670 680 690 700
VAASGEVAAE GSDGPLRAGE SATIALPAMP AAPLGETWLT VEAVLRDATG
710 720 730 740 750
WAPAGHPLGA VQLDLSAPAV PTRSPRPATP LDGALPVSLG PATFDAGTLV
760 770 780 790 800
SLAGQPVSGP RLELWRAPTD NDRGAGFGAY GPGDPWLNSG RGVPAPSSEA
810 820 830 840 850
VWKQAGLDRL TRRVEDVAAL PDGIRVRTRY AAADSTHSVA VEENWQLDGG
860 870 880 890 900
ELCLRIDITP SAGWNLVWPR IGVRWDLPTD VDGAAWFGAG PRESYPDSMH
910 920 930 940 950
ATVVARHAAS LEELNVPYAR PQETGHRSDV RWLELDRAGA PWLRIDAEPD
960 970 980 990 1000
AAGRRPGFSL ARHTAQEIAA AGHPHELPTP SHSYLYVDAA QHGLGSRACG
1010 1020
PDVWPDFALR PEARTLKLRI SPA
Length:1,023
Mass (Da):110,855
Last modified:October 1, 2002 - v1
Checksum:iFB7B7C2DE803988A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ457162 Genomic DNA. Translation: CAD29775.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ457162 Genomic DNA. Translation: CAD29775.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YQ2X-ray1.90A/B/C/D/E/F1-1023[»]
ProteinModelPortaliQ8KRF6.
SMRiQ8KRF6. Positions 4-1023.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ8KRF6.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR004199. B-gal_small/dom_5.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. GH-type_carb-bd.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR006103. Glyco_hydro_2_cat.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR032312. LacZ_4.
[Graphical view]
PfamiPF02929. Bgal_small_N. 1 hit.
PF16353. DUF4981. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]
PRINTSiPR00132. GLHYDRLASE2.
SMARTiSM01038. Bgal_small_N. 1 hit.
[Graphical view]
SUPFAMiSSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEiPS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The cloning, purification and characterization of a cold active beta-galactosidase from the psychrotolerant Antarctic bacterium Arthrobacter sp. C2-2."
    Karasova P., Strnad H., Spiwok V., Mala S., Kralova B., Russell N.J.
    Enzyme Microb. Technol. 33:836-844(2003)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C2-2Imported.
  2. "Cold-active beta-galactosidase from Arthrobacter sp. C2-2 forms compact 660 kDa hexamers: crystal structure at 1.9A resolution."
    Skalova T., Dohnalek J., Spiwok V., Lipovova P., Vondrackova E., Petrokova H., Duskova J., Strnad H., Kralova B., Hasek J.
    J. Mol. Biol. 353:282-294(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.

Entry informationi

Entry nameiQ8KRF6_9MICC
AccessioniPrimary (citable) accession number: Q8KRF6
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2002
Last sequence update: October 1, 2002
Last modified: July 6, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.