ID A0A0D5ZC59_PAEPS Unreviewed; 850 AA.
AC A0A0D5ZC59;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 Name=bmnA {ECO:0000313|EMBL:AKA44223.1};
GN ORFNames=PPSC2_09340 {ECO:0000313|EMBL:AKA44223.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:AKA44223.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:AKA44223.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:AKA44223.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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}.
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DR EMBL; CP002213; AKA44223.1; -; Genomic_DNA.
DR RefSeq; WP_014599645.1; NC_014622.2.
DR AlphaFoldDB; A0A0D5ZC59; -.
DR STRING; 1406.LK13_21810; -.
DR KEGG; ppm:PPSC2_09340; -.
DR PATRIC; fig|886882.15.peg.1967; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_3_2_9; -.
DR OrthoDB; 9801077at2; -.
DR Proteomes; UP000006868; Chromosome.
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 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; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
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; PF17753; Ig_mannosidase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 3.
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:UP000006868};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 199..303
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 675..761
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 765..846
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 850 AA; 97158 MW; 0AC4E064F8C8A3AF CRC64;
MINVIGLDGW RFREAHSDEW LSAKVPGCVH TDLLRHGKIL DPFIGMNEME VQWIDKQDWI
YEAYFEIDAN QLQCRCVELV LEGLDTYADV RVNGQTVISA NNMFRVWRQD VKAFVQQGKN
RLEIHFRSPI TEDVPKLERL GYGLPAPNDQ SEIGGLSDKK VSVFARKAPY HYGWDWGPRL
VTSGIWREVR IEAWSGLVVR DLFIRQDKVS TERAELTAMV EIESANEIRD AELCISADGR
VWSKPVRLLK GKQTVELELD MKEPKLWWCR GLGEPHQYTF VAELKEQAQE AVIAEKSVKT
GLRSIRLIRE RDTAGESFYF ELNGIPVFVK GANHIPNDSF AAEVTLERYR HEIASAAASH
MNMLRVWGGG IYEEDVFYDL CDEYGLLVWQ DFMFACSMYP GDQAFLDNVA QEAEDNIKRL
RHHPCIALWC GNNEIDSAWA HYEENAGWGW KKAYTPEQRE RLWEDYETLF HRILPEAVNA
WTPQTAYWPS SPLIDLTGDR NQHAHPSSTA GDIHYWGVWH ASEPFENYHV HVGRFMSEYG
FQSFPEYKSV RAYAEEKDLE LESEVMLAHQ KNGSGNRLIQ EYMGRYMRQP KDFPCFLLMS
QVLQAEAMKM AIEAHRRHKP YCMGTLYWQM NDCWPVASWS SMDYFGRWKA LQYTAKRSFA
DVLLSAVDTE QGSKELHLVN DTLEPIAGTL RLTLLHIRGS QAIREENIKV EQQAGGAGIV
HILPTDKWLN GLDRTEHMLV ARLIQNGEQV AASEIYFAGT KEMDLPQAKI EVTEIPGSGG
SRFTLCSDVL ARHVWLTAEQ EGIFSDNHLD LAPGVPKTVE FLALRNGASA FEVAAPGALT
VQSLINWIQG
//
