P36924

PR
Gene name
spoII
Protein name
Beta-amylase
Names
1,4-alpha-D-glucan maltohydrolase
Species
Bacillus cereus
KEGG Pathway
EC number
3.2.1.2: 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)

1-62 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

16 structures for P36924

Entry ID Method Resolution Chain Position Source
1B90 X-ray 250 A A 31-546 PDB
1B9Z X-ray 210 A A 31-546 PDB
1CQY X-ray 195 A A 448-546 PDB
1ITC X-ray 210 A A 31-546 PDB
1J0Y X-ray 210 A A/B/C/D 31-546 PDB
1J0Z X-ray 220 A A/B/C/D 31-546 PDB
1J10 X-ray 210 A A/B/C/D 31-546 PDB
1J11 X-ray 200 A A/B/C/D 31-546 PDB
1J12 X-ray 210 A A/B/C/D 31-546 PDB
1J18 X-ray 200 A A 31-546 PDB
1VEM X-ray 185 A A 31-546 PDB
1VEN X-ray 202 A A 31-546 PDB
1VEO X-ray 212 A A 31-546 PDB
1VEP X-ray 206 A A 31-546 PDB
5BCA X-ray 220 A A/B/C/D 31-546 PDB
AF-P36924-F1 Predicted AlphaFoldDB

No variants for P36924

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P36924

No associated diseases with P36924

4 regional properties for P36924

Type Name Position InterPro Accession
domain Carbohydrate binding module family 20 444 - 546 IPR002044
conserved_site Glycoside hydrolase, family 14, conserved site 119 - 127 IPR018238-1
conserved_site Glycoside hydrolase, family 14, conserved site 198 - 208 IPR018238-2
domain Beta-amylase, CBM20 domain 448 - 546 IPR034835

Functions

Description
EC Number 3.2.1.2 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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
amylopectin maltohydrolase activity Catalysis of the reaction: n H2O + an exposed unphosphorylated, unbranched malto-oligosaccharide tail on amylopectin <=> amylopectin + maltose.
beta-amylase activity Catalysis of the reaction: (1,4-alpha-D-glucosyl)(n+1) + H2O = (1,4-alpha-D-glucosyl)(n-1) + alpha-maltose. This reaction is the hydrolysis of 1,4-alpha-glucosidic linkages in polysaccharides so as to remove successive maltose units from the non-reducing ends of the chains.
metal ion binding Binding to a metal ion.
starch binding Binding to starch.

1 GO annotations of biological process

Name Definition
polysaccharide catabolic process The chemical reactions and pathways resulting in the breakdown of a polysaccharide, a polymer of many (typically more than 10) monosaccharide residues linked glycosidically.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKNQFQYCCI VILSVVMLFV SLLIPQASSA AVNGKGMNPD YKAYLMAPLK KIPEVTNWET
70 80 90 100 110 120
FENDLRWAKQ NGFYAITVDF WWGDMEKNGD QQFDFSYAQR FAQSVKNAGM KMIPIISTHQ
130 140 150 160 170 180
CGGNVGDDCN VPIPSWVWNQ KSDDSLYFKS ETGTVNKETL NPLASDVIRK EYGELYTAFA
190 200 210 220 230 240
AAMKPYKDVI AKIYLSGGPA GELRYPSYTT SDGTGYPSRG KFQAYTEFAK SKFRLWVLNK
250 260 270 280 290 300
YGSLNEVNKA WGTKLISELA ILPPSDGEQF LMNGYLSMYG KDYLEWYQGI LENHTKLIGE
310 320 330 340 350 360
LAHNAFDTTF QVPIGAKIAG VHWQYNNPTI PHGAEKPAGY NDYSHLLDAF KSAKLDVTFT
370 380 390 400 410 420
CLEMTDKGSY PEYSMPKTLV QNIATLANEK GIVLNGENAL SIGNEEEYKR VAEMAFNYNF
430 440 450 460 470 480
AGFTLLRYQD VMYNNSLMGK FKDLLGVTPV MQTIVVKNVP TTIGDTVYIT GNRAELGSWD
490 500 510 520 530 540
TKQYPIQLYY DSHSNDWRGN VVLPAERNIE FKAFIKSKDG TVKSWQTIQQ SWNPVPLKTT
SHTSSW