ID A9AYF0_HERA2 Unreviewed; 823 AA.
AC A9AYF0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
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 OrderedLocusNames=Haur_0884 {ECO:0000313|EMBL:ABX03532.1};
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexota; Chloroflexia; Herpetosiphonales;
OC Herpetosiphonaceae; Herpetosiphon.
OX NCBI_TaxID=316274 {ECO:0000313|EMBL:ABX03532.1, ECO:0000313|Proteomes:UP000000787};
RN [1] {ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABX03532.1, ECO:0000313|Proteomes:UP000000787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95
RC {ECO:0000313|Proteomes:UP000000787};
RX PubMed=22675585; DOI=10.4056/sigs.2194987;
RA Kiss H., Nett M., Domin N., Martin K., Maresca J.A., Copeland A.,
RA Lapidus A., Lucas S., Berry K.W., Glavina Del Rio T., Dalin E., Tice H.,
RA Pitluck S., Richardson P., Bruce D., Goodwin L., Han C., Detter J.C.,
RA Schmutz J., Brettin T., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA Goker M., Woyke T., Klenk H.P., Bryant D.A.;
RT "Complete genome sequence of the filamentous gliding predatory bacterium
RT Herpetosiphon aurantiacus type strain (114-95(T)).";
RL Stand. Genomic Sci. 5:356-370(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; CP000875; ABX03532.1; -; Genomic_DNA.
DR AlphaFoldDB; A9AYF0; -.
DR STRING; 316274.Haur_0884; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; hau:Haur_0884; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_005015_1_1_0; -.
DR InParanoid; A9AYF0; -.
DR BioCyc; HAUR316274:GHYA-898-MONOMER; -.
DR Proteomes; UP000000787; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004567; F:beta-mannosidase activity; IEA:UniProtKB-EC.
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; 2.
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; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:ABX03532.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABX03532.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 196..301
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 665..747
FT /note="Mannosidase Ig/CBM-like"
FT /evidence="ECO:0000259|Pfam:PF17786"
FT DOMAIN 752..802
FT /note="Beta-mannosidase Ig-fold"
FT /evidence="ECO:0000259|Pfam:PF17753"
SQ SEQUENCE 823 AA; 92458 MW; 7F0DE64F33FB9F83 CRC64;
MQKLALQQAW QAKQRDPQRT VLADSTSSEG WIAAPVPGTI YEALIAAERI PDPFDGLNEL
AVQWVAEVDW LYRCDFELTA EQANQPAALH FAGLDTIATV WINGQEILNS DNMFVPQRVV
VSNQIHVGAN QLLIEFRSAL KHGHALQAEM GQLGVWNGDP SRLYLRKAQY HYGWDWGPAL
LTAGPWLPVT LELGATRLSD LACPISVADD CSTAIFAVTA TVADVQADTA VLIQLWNPAG
ELIAEHQQLV VAGNIQHSIT VDQPSLWWPH GYGQQHRYRL AVKVFANQTV LDQQELQLGV
RRVRLVQEPL LDEAGETFLF EINNVPMFSG GANWIPADLL TNRVSNEHYR RLLQAAVDSH
MLMIRIWGGG IYEVDHFYDL CDQLGLLVWQ DFMFACGMYP AHPAFLASVE AEAIAQVQRL
RHHPSIVLWC GNNEDYQIAQ TFNAYDHSFQ GDFTKTSFPA REIYERLLPK VCASYDPTTI
YWPGSPYGGA DVYDKTRGDR HTWDVWHSAM APYQDYPKYE GRFVSEFGME SCAALPTLLS
VIPEHERYPQ SRTVEHHNKS EGGARRLAVY LNDTLRFENT LESYVYATQL MQAEALAAAY
RGWRRRWGGA GRYAVAGALV WQLNDCWPVI SWAIIDSALR KKPAIYSIGR ELAPISAGLQ
RNGATIEAWV VNGTIESKSA TIQLTGYDLH GRLLFEQNIE YELAANQANP IPSPNLNLPE
QSVVGMQVLV DGVVVARASA WPEPFKYLPA YDPQISVTRM ADDWLEISSQ HPAKGVWLQT
EAEINWSDNL LDLLPNQPQR IQACGLGQQP IDIKWLHWDQ ART
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