Q56307

PR
Gene name
lacZ (TM_1193)
Protein name
Beta-galactosidase
Names
Beta-gal, Lactase
Species
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
KEGG Pathway
tma:TM1193
EC number
3.2.1.23: Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

215-294 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

3 structures for Q56307

Entry ID Method Resolution Chain Position Source
6S6Z EM 210 A A/B/C/D/E/F/G/H 2-1084 PDB
6SD0 X-ray 370 A A/B/C/D 1-1084 PDB
AF-Q56307-F1 Predicted AlphaFoldDB

No variants for Q56307

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q56307

No associated diseases with Q56307

7 regional properties for Q56307

Type Name Position InterPro Accession
domain Beta galactosidase small chain/ domain 5 715 - 981 IPR004199
domain Glycoside hydrolase, family 2, immunoglobulin-like beta-sandwich 211 - 311 IPR006102
domain Glycoside hydrolase family 2, catalytic domain 313 - 599 IPR006103
domain Glycosyl hydrolases family 2, sugar binding domain 41 - 208 IPR006104
conserved_site Glycoside hydrolase, family 2, conserved site 363 - 388 IPR023230
active_site Glycoside hydrolase, family 2, active site 427 - 441 IPR023232
domain Beta-galactosidase, domain 4 608 - 691 IPR032312

Functions

Description
EC Number 3.2.1.23 Glycosidases, ie enzymes hydrolyzing O- and S-glycosyl compounds
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
beta-galactosidase complex A protein complex that possesses beta-galactosidase activity, i.e. catalyzes the hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides. In E. coli, the complex is a homotetramer; dimeric and hexameric beta-galactosidase complexes have been observed in other species.

2 GO annotations of molecular function

Name Definition
beta-galactosidase activity Catalysis of the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-D-galactosides.
carbohydrate binding Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.

1 GO annotations of biological process

Name Definition
lactose catabolic process The chemical reactions and pathways resulting in the breakdown of lactose, the disaccharide galactopyranosyl-glucose.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPYEWENPQL VSEGTEKSHA SFIPYLDPFS GEWEYPEEFI SLNGNWRFLF AKNPFEVPED
70 80 90 100 110 120
FFSEKFDDSN WDEIEVPSNW EMKGYGKPIY TNVVYPFEPN PPFVPKDDNP TGVYRRWIEI
130 140 150 160 170 180
PEDWFKKEIF LHFEGVRSFF YLWVNGKKIG FSKDSCTPAE FRLTDVLRPG KNLITVEVLK
190 200 210 220 230 240
WSDGSYLEDQ DMWWFAGIYR DVYLYALPKF HIRDVFVRTD LDENYRNGKI FLDVEMRNLG
250 260 270 280 290 300
EEEEKDLEVT LITPDGDEKT LVKETVKPED RVLSFAFDVK DPKKWSAETP HLYVLKLKLG
310 320 330 340 350 360
EDEKKVNFGF RKIEIKDGTL LFNGKPLYIK GVNRHEFDPD RGHAVTVERM IQDIKLMKQH
370 380 390 400 410 420
NINTVRTSHY PNQTKWYDLC DYFGLYVIDE ANIESHGIDW DPEVTLANRW EWEKAHFDRI
430 440 450 460 470 480
KRMVERDKNH PSIIFWSLGN EAGDGVNFEK AALWIKKRDN TRLIHYEGTT RRGESYYVDV
490 500 510 520 530 540
FSLMYPKMDI LLEYASKKRE KPFIMCEYAH AMGNSVGNLK DYWDVIEKYP YLHGGCIWDW
550 560 570 580 590 600
VDQGIRKKDE NGREFWAYGG DFGDTPNDGN FCINGVVLPD RTPEPELYEV KKVYQNVKIR
610 620 630 640 650 660
QVSKDTYEVE NRYLFTNLEM FDGAWKIRKD GEVIEEKTFK IFAEPGEKRL LKIPLPEMDD
670 680 690 700 710 720
SEYFLEISFS LSEDTPWAEK GHVVAWEQFL LKAPAFEKKS ISDGVSLRED GKHLTVEAKD
730 740 750 760 770 780
TVYVFSKLTG LLEQILHRRK KILKSPVVPN FWRVPTDNDI GNRMPQRLAI WKRASKERKL
790 800 810 820 830 840
FKMHWKKEEN RVSVHSVFQL PGNSWVYTTY TVFGNGDVLV DLSLIPAEDV PEIPRIGFQF
850 860 870 880 890 900
TVPEEFGTVE WYGRGPHETY WDRKESGLFA RYRKAVGEMM HRYVRPQETG NRSDVRWFAL
910 920 930 940 950 960
SDGETKLFVS GMPQIDFSVW PFSMEDLERV QHISELPERD FVTVNVDFRQ MGLGGDDSWG
970 980 990 1000 1010 1020
AMPHLEYRLL PKPYRFSFRM RISEEIPSWR VLAAIPETLH VEMSSEDVIR EGDTLRVKFS
1030 1040 1050 1060 1070 1080
LLNDTPLSKE KQVVLFVDGN EYSVRRVVIP PFKKEELVFK VEGLKKGEHL IHTNLNTRKT
IYVR