Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A9R0J8

- BGAL_YERPG

UniProt

A9R0J8 - BGAL_YERPG

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-galactosidase

Gene

lacZ

Organism
Yersinia pestis bv. Antiqua (strain Angola)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotationNote: Binds 2 magnesium ions per monomer.UniRule annotation
  • Na(+)UniRule annotationNote: Binds 1 sodium ion per monomer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001SubstrateUniRule annotation
Metal bindingi199 – 1991SodiumUniRule annotation
Binding sitei199 – 1991SubstrateUniRule annotation
Sitei363 – 3631Transition state stabilizerUniRule annotation
Sitei397 – 3971Transition state stabilizerUniRule annotation
Metal bindingi422 – 4221Magnesium 1UniRule annotation
Metal bindingi424 – 4241Magnesium 1UniRule annotation
Active sitei467 – 4671Proton donorUniRule annotation
Metal bindingi467 – 4671Magnesium 1UniRule annotation
Binding sitei467 – 4671SubstrateUniRule annotation
Active sitei543 – 5431NucleophileUniRule annotation
Metal bindingi603 – 6031Magnesium 2UniRule annotation
Metal bindingi607 – 6071Sodium; via carbonyl oxygenUniRule annotation
Metal bindingi610 – 6101SodiumUniRule annotation
Binding sitei610 – 6101SubstrateUniRule annotation
Binding sitei1025 – 10251SubstrateUniRule annotation

GO - Molecular functioni

  1. beta-galactosidase activity Source: UniProtKB-EC
  2. carbohydrate binding Source: InterPro
  3. magnesium ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Sodium

Enzyme and pathway databases

BioCyciYPES349746:GHPB-2840-MONOMER.

Protein family/group databases

CAZyiGH2. Glycoside Hydrolase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-galactosidaseUniRule annotation (EC:3.2.1.23UniRule annotation)
Short name:
Beta-galUniRule annotation
Alternative name(s):
LactaseUniRule annotation
Gene namesi
Name:lacZUniRule annotation
Ordered Locus Names:YpAngola_A2834
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001204: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. beta-galactosidase complex Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10501050Beta-galactosidasePRO_0000367017Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi349746.YpAngola_A2834.

Structurei

3D structure databases

ProteinModelPortaliA9R0J8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni543 – 5464Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the glycosyl hydrolase 2 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3250.
HOGENOMiHOG000252443.
KOiK01190.
OMAiNPPFVPK.
OrthoDBiEOG6XWV0T.

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.
HAMAPiMF_01687. Beta_gal.
InterProiIPR004199. B-gal_small/dom_5.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR023933. Glyco_hydro_2_beta_Galsidase.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF02929. Bgal_small_N. 1 hit.
PF00703. Glyco_hydro_2. 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.

A9R0J8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLSLPQILS RRDWENPQIT QYHRLEAHPP FHSWRDVESA QKDRPSPQQQ
60 70 80 90 100
TLNGLWSFSY FTQPEAVPEH WVRCDLAEAK PLPVPANWQL HGYDAPIYTN
110 120 130 140 150
IQYPIPVNPP RVPDLNPTGC YSRDFTLEPS WLASGKTRII FDGVSSAFYL
160 170 180 190 200
WCNGQWVGYS QDSRLPAEFD LTPYLQAGSN RIAVLVLRWS DGSYLEDQDM
210 220 230 240 250
WRMSGIFRDV KLLHKPEIHL RDIHIMTHLS PEFTSANLEV MAAVNIPSLQ
260 270 280 290 300
LNDPQVTGSY QLRVQLWLAD KLVASLQQPL GTQAIDERGP YTDRTQLVLR
310 320 330 340 350
IDQPLLWSAE QPTLYRAVVS LLNHQQELIE AEAYDVGFRQ VAIHQGLLKI
360 370 380 390 400
NGKAVLIRGV NRHEHHPQTG QAIDEESLLQ DILLMKQHNF NAVRCSHYPN
410 420 430 440 450
HPLWYRLCDR YGLYVVDEAN IETHGMQPMS RLSDDPSWFS AFSERVTRMV
460 470 480 490 500
QRDRNHPCII IWSLGNESGH GATHDALYRW IKTNDPTRPV QYEGGGANTL
510 520 530 540 550
ATDILCPMYA RVDEDQPFPA VPKWSIKKWI GLPNESRPLI LCEYAHAMGN
560 570 580 590 600
SFGGFARYWQ AFRQYPRLQG GFIWDWVDQS LTHHNDHGQP YWAYGGDFGD
610 620 630 640 650
TPNDRQFCMN GLVFPDRSPH PSLYEAQCAQ QFFQFSLLST TPLVINITSE
660 670 680 690 700
YLFRESDNEQ LYWRIMLEGE SVLEGSQPLN LSPESSQCYR LAEKLPTLNK
710 720 730 740 750
PGQLWLNVEI RQPKETPWSP AQHRSAWHQW RLPQPLFSPS SDLTNATAHY
760 770 780 790 800
APQLQHNLQL QHDLQLQQDE QHIKVTYQQQ CWQFSRQTGR LAQWWVADKP
810 820 830 840 850
MLLRPLQDQF VRAPLDNDIG ISEATHIDPN AWVERWKKAG MYQLQQRCLS
860 870 880 890 900
LHVDHLSHSV QISAEYGYEF EQEPLLHSHW VYRFDRHGRM TIDVNVRIAT
910 920 930 940 950
SLPAPARIGM CCQLADISPT VEWLGLGPHE NYPDRQLAAQ YGHWSLPLEQ
960 970 980 990 1000
MHTAYIFPSE NGLRCNTHTL NYGRWTLTGD FHFGISRYST QQLMVTSHQH
1010 1020 1030 1040 1050
LLEPEEGTWL NIDGFHMGVG GDDSWSPSVH IDDILTRETY QYQICWQYKV
Length:1,050
Mass (Da):121,515
Last modified:February 5, 2008 - v1
Checksum:i4B4462FF07D85F61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX87965.1.
RefSeqiYP_001607216.1. NC_010159.1.

Genome annotation databases

EnsemblBacteriaiABX87965; ABX87965; YpAngola_A2834.
GeneIDi5801306.
KEGGiypg:YpAngola_A2834.
PATRICi18575175. VBIYerPes97331_3350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000901 Genomic DNA. Translation: ABX87965.1 .
RefSeqi YP_001607216.1. NC_010159.1.

3D structure databases

ProteinModelPortali A9R0J8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349746.YpAngola_A2834.

Protein family/group databases

CAZyi GH2. Glycoside Hydrolase Family 2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX87965 ; ABX87965 ; YpAngola_A2834 .
GeneIDi 5801306.
KEGGi ypg:YpAngola_A2834.
PATRICi 18575175. VBIYerPes97331_3350.

Phylogenomic databases

eggNOGi COG3250.
HOGENOMi HOG000252443.
KOi K01190.
OMAi NPPFVPK.
OrthoDBi EOG6XWV0T.

Enzyme and pathway databases

BioCyci YPES349746:GHPB-2840-MONOMER.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
2.60.40.320. 2 hits.
2.70.98.10. 1 hit.
3.20.20.80. 1 hit.
HAMAPi MF_01687. Beta_gal.
InterProi IPR004199. B-gal_small/dom_5.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR006101. Glyco_hydro_2.
IPR013812. Glyco_hydro_2/20_Ig-like.
IPR023232. Glyco_hydro_2_AS.
IPR023933. Glyco_hydro_2_beta_Galsidase.
IPR023230. Glyco_hydro_2_CS.
IPR006102. Glyco_hydro_2_Ig-like.
IPR006104. Glyco_hydro_2_N.
IPR006103. Glyco_hydro_2_TIM.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF02929. Bgal_small_N. 1 hit.
PF00703. Glyco_hydro_2. 1 hit.
PF02836. Glyco_hydro_2_C. 1 hit.
PF02837. Glyco_hydro_2_N. 1 hit.
[Graphical view ]
PRINTSi PR00132. GLHYDRLASE2.
SMARTi SM01038. Bgal_small_N. 1 hit.
[Graphical view ]
SUPFAMi SSF49303. SSF49303. 2 hits.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEi PS00719. GLYCOSYL_HYDROL_F2_1. 1 hit.
PS00608. GLYCOSYL_HYDROL_F2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
    Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
    J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Angola.

Entry informationi

Entry nameiBGAL_YERPG
AccessioniPrimary (citable) accession number: A9R0J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: November 26, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3