Q8KRF6 (Q8KRF6_9MICC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Beta-galactosidase EMBL CAD29775.1
EC=3.2.1.23 EMBL CAD29775.1

Gene names

Name:

lacZ EMBL CAD29775.1

Organism

Arthrobacter sp. C2-2 EMBL CAD29775.1

Taxonomic identifier

192168 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter

Protein attributes

Sequence length	1023 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. SAAS SAAS023230

Ontologies

Keywords
Ligand	Magnesium PDB 1YQ2 Metal-binding PDB 1YQ2
Molecular function	Glycosidase SAAS SAAS023230 EMBL CAD29775.1 Hydrolase
Technical term	3D-structure PDB 1YQ2
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	beta-galactosidase complex Inferred from electronic annotation. Source: InterPro
Molecular function	beta-galactosidase activity Inferred from electronic annotation. Source: EC carbohydrate binding 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	525	1	Magnesium; via carbonyl oxygen PDB 1YQ2
	Metal binding	527	1	Magnesium; via carbonyl oxygen PDB 1YQ2
	Metal binding	529	1	Magnesium; via carbonyl oxygen PDB 1YQ2

Sequences

	Sequence		Length	Mass (Da)
	Q8KRF6 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: FB7B7C2DE803988A	FASTA	1,023	110,855
	10 20 30 40 50 60 MTTADVSYLT DQGPGSGRRV PARSWLHSDA PALSLNGDWR FRLLPAAPGT AGAGSVLPSG 70 80 90 100 110 120 ETVEGVAAES YDDAAWDTLP VPSHWVMGQD GKYGRPIYTN VQYPFPIDPP HVPDANPTGD 130 140 150 160 170 180 FRRRFDVPAQ WFESTTAALT LRFDGVESRY KVWVNGQEIG VGSGSRLAQE FDVSDALRAG 190 200 210 220 230 240 SNLLVVRVHQ WSAASYLEDQ DQWWLPGIFR DVTLQARPAG GITDAWLRTG WSARSGAGTG 250 260 270 280 290 300 TIDPEITADA TAFPVTLSVP ELGVNVTWKS AEEVAPLALE NVEPWSAEVP RLYEASVSSA 310 320 330 340 350 360 AESISVRLGF RTVRIVGDQF LVNGRRVVFH GVNRHETHPD RGRVFDEAGA REDLALMKRF 370 380 390 400 410 420 NVNAIRTSHY PPHPRLLDLA DEMGFWVILE CDLETHGFEA GGWVENPSDV PAWRDALVDR 430 440 450 460 470 480 MERTVERDKN HPSIVMWSLG NESGTGSNLA AMAAWAHARD SSRPVHYEGD YTGAYTDVYS 490 500 510 520 530 540 RMYSSIPETD SIGRNDSHAL LLGCDSAESA RQRTKPFILC EYVHAMGNGP GAMDQYEALV 550 560 570 580 590 600 DKYPRLHGGF VWEWRDHGIR TRTAEGMEFF AYGGDFGEVV HDSNFVMDGM VLSDSTPTPG 610 620 630 640 650 660 LYEFKQIVSP IRLGLSLPAG GKPTLAVANL RHTADASDVV LRWRVEHDGA VAASGEVAAE 670 680 690 700 710 720 GSDGPLRAGE SATIALPAMP AAPLGETWLT VEAVLRDATG WAPAGHPLGA VQLDLSAPAV 730 740 750 760 770 780 PTRSPRPATP LDGALPVSLG PATFDAGTLV SLAGQPVSGP RLELWRAPTD NDRGAGFGAY 790 800 810 820 830 840 GPGDPWLNSG RGVPAPSSEA VWKQAGLDRL TRRVEDVAAL PDGIRVRTRY AAADSTHSVA 850 860 870 880 890 900 VEENWQLDGG ELCLRIDITP SAGWNLVWPR IGVRWDLPTD VDGAAWFGAG PRESYPDSMH 910 920 930 940 950 960 ATVVARHAAS LEELNVPYAR PQETGHRSDV RWLELDRAGA PWLRIDAEPD AAGRRPGFSL 970 980 990 1000 1010 1020 ARHTAQEIAA AGHPHELPTP SHSYLYVDAA QHGLGSRACG PDVWPDFALR PEARTLKLRI SPA

References

[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: C2-2 EMBL CAD29775.1.
[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: 16171818] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ457162 Genomic DNA. Translation: CAD29775.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YQ2	X-ray	1.90	A/B/C/D/E/F	1-1023	[»]

ProteinModelPortal

Q8KRF6.

SMR

Q8KRF6. Positions 4-1023.

ModBase

Search...

Protein family/group databases

CAZy

GH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR004199. B-gal_small/dom_5.
IPR008979. Galactose-bd-like.
IPR011013. Glyco_hydro-type_carb-bd.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:2.60.40.320. Glyco_hydro_2/20_Ig-like. 2 hits.
G3DSA:2.70.98.10. Glyco_hydro_42_D5. 1 hit.
G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF02929. Bgal_small_N. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view]

PRINTS

PR00132. GLHYDRLASE2.

SMART

SM01038. Bgal_small_N. 1 hit.
[Graphical view]

SUPFAM

SSF49785. Gal_bind_like. 1 hit.
SSF74650. Gal_mut_like. 1 hit.
SSF49303. Glyco_hydro_2Ig. 2 hits.
SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q8KRF6_9MICC

Accession

Primary (citable) accession number: Q8KRF6

Entry history

Integrated into UniProtKB/TrEMBL:	October 1, 2002
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)