ID A0A2S8SRX4_9BACT Unreviewed; 824 AA. AC A0A2S8SRX4; DT 18-JUL-2018, integrated into UniProtKB/TrEMBL. DT 18-JUL-2018, sequence version 1. DT 27-NOV-2024, entry version 20. DE RecName: Full=Beta-mannosidase B {ECO:0000256|ARBA:ARBA00041069}; DE EC=3.2.1.25 {ECO:0000256|ARBA:ARBA00012754}; DE AltName: Full=Mannanase B {ECO:0000256|ARBA:ARBA00041614}; GN ORFNames=B1R32_11187 {ECO:0000313|EMBL:PQV63526.1}; OS Abditibacterium utsteinense. OC Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales; OC Abditibacteriaceae; Abditibacterium. OX NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV63526.1, ECO:0000313|Proteomes:UP000237684}; RN [1] {ECO:0000313|EMBL:PQV63526.1, ECO:0000313|Proteomes:UP000237684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV63526.1, RC ECO:0000313|Proteomes:UP000237684}; RX PubMed=29475572; RA Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.; RT "Abditibacterium utsteinense sp. nov., the first cultivated member of RT candidate phylum FBP, isolated from ice-free Antarctic soil samples."; RL Syst. Appl. Microbiol. 0:0-0(2018). CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal, non-reducing beta-D-mannose residues CC in beta-D-mannosides.; EC=3.2.1.25; CC Evidence={ECO:0000256|ARBA:ARBA00000829}; CC -!- PATHWAY: Glycan metabolism; N-glycan degradation. CC {ECO:0000256|ARBA:ARBA00004740}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. Beta- CC mannosidase B subfamily. {ECO:0000256|ARBA:ARBA00038429}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PQV63526.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; NIGF01000011; PQV63526.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2S8SRX4; -. DR InParanoid; A0A2S8SRX4; -. DR OrthoDB; 9801077at2; -. DR Proteomes; UP000237684; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProt. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006516; P:glycoprotein catabolic process; IEA:TreeGrafter. DR FunFam; 3.20.20.80:FF:000050; Beta-mannosidase B; 1. DR FunFam; 2.60.120.260:FF:000060; Probable beta-mannosidase; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR InterPro; IPR036156; Beta-gal/glucu_dom_sf. DR InterPro; IPR054593; Beta-mannosidase-like_N2. DR InterPro; IPR050887; Beta-mannosidase_GH2. DR InterPro; IPR041625; Beta-mannosidase_Ig. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR006102; Glyco_hydro_2_Ig-like. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR041447; Mannosidase_ig. DR PANTHER; PTHR43730; BETA-MANNOSIDASE; 1. DR PANTHER; PTHR43730:SF1; BETA-MANNOSIDASE; 1. DR Pfam; PF00703; Glyco_hydro_2; 1. DR Pfam; PF22666; Glyco_hydro_2_N2; 1. DR Pfam; PF17753; Ig_mannosidase; 1. DR Pfam; PF17786; Mannosidase_ig; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. PE 3: Inferred from homology; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Reference proteome {ECO:0000313|Proteomes:UP000237684}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}. FT DOMAIN 11..177 FT /note="Beta-mannosidase-like galactose-binding" FT /evidence="ECO:0000259|Pfam:PF22666" FT DOMAIN 233..282 FT /note="Glycoside hydrolase family 2 immunoglobulin-like FT beta-sandwich" FT /evidence="ECO:0000259|Pfam:PF00703" FT DOMAIN 649..733 FT /note="Mannosidase Ig/CBM-like" FT /evidence="ECO:0000259|Pfam:PF17786" FT DOMAIN 741..820 FT /note="Beta-mannosidase Ig-fold" FT /evidence="ECO:0000259|Pfam:PF17753" SQ SEQUENCE 824 AA; 94402 MW; D2317F5999A0FAEB CRC64; MILALPLHDG WTFRHADSAR NYPAQVPGCI HTDLLHNQLI PDPFWGANEL DLQWIEERNW SYSLKFRVEA SLLKRERVEL VCEGLDTLAT LVLNGHEIAR TENMFVGYRF EIKELLRQGE NELQIHFASP MPLIRERQKA HPGDEWNDPT GGSSNIRKEQ CSFGWDWGPR FATCGIYLPI RLESWNSNRI ESVHLAQKHE ANRVFLSLRP ALSQEAPDAH FRVQLRLNGS TLLETESLQF EVPSPQLWWC YGLGEQPLYE LSVELMSGDE VIDTWQKRIG LRTVELDRHA DEWGESFQFV VNGVPIFAKG ANWIPAHAFV TEAKREDYAG LLQSATDAHM NMIRVWGGGI YEMEDFYDLC DQKGLLVWQD FAFACGTYPG DEAFLNSVRE EADYQVERLQ HRACIALWCG NNEIEEGFRK TILSTPERKR AYQAIFDEVL PAAVEKFDGT RAYWPSSPHH PAGLDVEMNH ETGGDTHYWD VWHSRAPVKN YEKTNFRFCS EFGMQSYSSP EVAAQFCEPS QMNVFSPAME NHQKNPAGNQ IILDYISRQY RFPKDYASLA YLSQLNQAFT LKVGIEHFRR SMPRTMGALY WQLNDCWPVF SWSSLEFGGK WKALHFEAKR FFAPALISLF VPGDETAGIS NRITSTIHDV HIFTVYDGLG DKSGTIFWEL RHLDGRILES GSKAVELRYG ESINQKSLDF AGAMSQYGAK TLYVRAWLEI GGKVVSRQTA FLTARRFLEM PRAAIESQIQ ARGGSEYFFT FTSPVFQTQV QFELEGLSYR ASDNFFDLYP DVPHLVTVQL KNEFSPAEVA QRLSTMSLAD SYQS //