Q2TXB7

PR
Gene name
mndB (AO090010000208)
Protein name
Beta-mannosidase B
Names
Mannanase B, Mannase B
Species
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
KEGG Pathway
EC number
3.2.1.25: 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)

1-67 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q2TXB7

Entry ID Method Resolution Chain Position Source
AF-Q2TXB7-F1 Predicted AlphaFoldDB

No variants for Q2TXB7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2TXB7

No associated diseases with Q2TXB7

2 regional properties for Q2TXB7

Type Name Position InterPro Accession
domain Glycoside hydrolase, family 2, immunoglobulin-like beta-sandwich 196 - 301 IPR006102
domain Mannosidase Ig/CBM-like domain 679 - 767 IPR041447

Functions

Description
EC Number 3.2.1.25 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

1 GO annotations of molecular function

Name Definition
beta-mannosidase activity Catalysis of the hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides.

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
MAAFSQYPLS TGWSFKDSDD QSPEAWMPVP VVPSVAHQDL QANQKLKNPY IGFNELDARW
70 80 90 100 110 120
VNDKSWTYRT VFQKPAVAAG SSIILAFDGL DTFATVKLDG SVILQSDNMF LAHRVDVTKA
130 140 150 160 170 180
LEAEGDHVLE IDFDCAMRRA RELREKDTKH NWASFNGDPA RMAVRKAQYH WGWDWGPLLS
190 200 210 220 230 240
TAGIWREVRL EVYSAKISDL WTEVELASDH QTARVSAFAE VDAADSVDSY KASFLLSLHG
250 260 270 280 290 300
KEVAREVATL KDKVANVTFD VTQPSLWWPN GYGDPALYEI SVSLEKEDCE IHSVSKKIGI
310 320 330 340 350 360
RTAELIQQPD RHGKSFFFRI NGVDVFCGGS CWIPADNLLP SITAERYRKW IELMVAGRQV
370 380 390 400 410 420
MIRVWGGGCY EDDSFYQACD ELGVLVWQDF MFGCGNYPTW PELLESIEKE ANYNVRRLRH
430 440 450 460 470 480
HPSIVVYVGN NEDYQVQESA GLVYDYEDKN PENWLKTDFP ARYIYEKLLP SVVEKLSPKT
490 500 510 520 530 540
VYHPGSPWGD GKITSDPTVG DMHQWNVWHG TQEKYQIFDT LGGRFNSEFG MEAFPHMSTI
550 560 570 580 590 600
EYFVENEADK YPQSHVLDFH NKADGHERRI ATYLVENLRT ATDLETYVYL TQVVQAETMM
610 620 630 640 650 660
FGYRGWRRQW GDERHCGGAL LWQLNDCWPT ISWAIVDYFL RPKPAFYAVA RVLKPIAVGV
670 680 690 700 710 720
RREHHDWSVT HAQPPKTSKY ELWIASSLQK ETVGTIELRF LSVNTGLDVR APILRDNVKI
730 740 750 760 770 780
VPNGTTNILE GVIDHKAQPE PHVLAARLWV DGEVTARDVD WPQPFKYLDL SDRGLEVNKV
790 800 810 820 830 840
SESGNEQKLL ITAKKPVKCL VFEERDGIRV SDSAMDIVPG DGQTVTVTGL KAGDAPLKYK
YLGQ