MANA_BIFAA
ID MANA_BIFAA Reviewed; 1002 AA.
AC A1A278;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000303|PubMed:23064345};
DE EC=3.2.1.78 {ECO:0000269|PubMed:23064345};
DE AltName: Full=Beta-mannanase {ECO:0000303|PubMed:23064345};
DE AltName: Full=Mannanase 26A {ECO:0000303|PubMed:23064345};
DE Short=Man26A {ECO:0000303|PubMed:23064345};
DE AltName: Full=Mannanase A {ECO:0000303|PubMed:23064345};
DE Short=ManA {ECO:0000303|PubMed:23064345};
DE Flags: Precursor;
GN OrderedLocusNames=BAD_1030;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, POLYSACCHARIDE-BINDING, BIOPHYSICOCHEMICAL
RP PROPERTIES, DOMAIN, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RX PubMed=23064345; DOI=10.1128/aem.02118-12;
RA Kulcinskaja E., Rosengren A., Ibrahim R., Kolenova K., Stalbrand H.;
RT "Expression and characterization of a Bifidobacterium adolescentis beta-
RT mannanase carrying mannan-binding and cell association motifs.";
RL Appl. Environ. Microbiol. 79:133-140(2013).
CC -!- FUNCTION: Beta-mannanase likely involved in the utilization of
CC carbohydrates in the human gut. Catalyzes the hydrolysis of different
CC beta-1,4-linked mannans, such as ivory nut mannan, konjac glucomannan,
CC as well as carob and guar gum galactomannans, to a mixture of
CC oligosaccharides. The dominant product from ivory nut mannan is found
CC to be mannotriose; mannobiose and mannotetraose are produced to a
CC lesser extent. Does not hydrolyze mannobiose, and hydrolyzes
CC mannotriose at a significantly lower rate than the longer
CC oligosaccharides. {ECO:0000269|PubMed:23064345}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in
CC mannans, galactomannans and glucomannans.; EC=3.2.1.78;
CC Evidence={ECO:0000269|PubMed:23064345};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.3. Retains over 90% of its activity in the pH range
CC of 5 to 6. {ECO:0000269|PubMed:23064345};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49424}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305}; Peptidoglycan-
CC anchor {ECO:0000305}. Note=Is likely to be cell attached, either by the
CC sortase mechanism (LPXTG motif) or via a C-terminal transmembrane
CC helix. {ECO:0000269|PubMed:23064345}.
CC -!- DOMAIN: The carbohydrate-binding modules (CBMs) are responsible for the
CC affinity to carob galactomannan. {ECO:0000269|PubMed:23064345}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family.
CC {ECO:0000255|PROSITE-ProRule:PRU01100, ECO:0000305}.
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; AP009256; BAF39811.1; -; Genomic_DNA.
DR RefSeq; WP_011743387.1; NC_008618.1.
DR AlphaFoldDB; A1A278; -.
DR SMR; A1A278; -.
DR STRING; 367928.BAD_1030; -.
DR CAZy; CBM23; Carbohydrate-Binding Module Family 23.
DR CAZy; GH26; Glycoside Hydrolase Family 26.
DR EnsemblBacteria; BAF39811; BAF39811; BAD_1030.
DR KEGG; bad:BAD_1030; -.
DR HOGENOM; CLU_297304_0_0_11; -.
DR OMA; HQHATTE; -.
DR Proteomes; UP000008702; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:2001065; F:mannan binding; IDA:UniProtKB.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IDA:UniProtKB.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR GO; GO:0051069; P:galactomannan metabolic process; ISS:UniProtKB.
DR GO; GO:0010391; P:glucomannan metabolic process; ISS:UniProtKB.
DR GO; GO:0046355; P:mannan catabolic process; IDA:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR005087; CBM_fam11.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR000805; Glyco_hydro_26.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR019931; LPXTG_anchor.
DR PANTHER; PTHR40079; PTHR40079; 1.
DR Pfam; PF03425; CBM_11; 2.
DR Pfam; PF02156; Glyco_hydro_26; 1.
DR PRINTS; PR00739; GLHYDRLASE26.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS51764; GH26; 1.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell wall; Glycosidase; Hydrolase;
KW Peptidoglycan-anchor; Polysaccharide degradation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1002
FT /note="Mannan endo-1,4-beta-mannosidase"
FT /id="PRO_0000424380"
FT PROPEP 970..1002
FT /note="Removed by sortase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT /id="PRO_0000424381"
FT DOMAIN 49..396
FT /note="GH26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01100"
FT DOMAIN 523..703
FT /note="CBM11 1"
FT /evidence="ECO:0000255"
FT DOMAIN 717..897
FT /note="CBM11 2"
FT /evidence="ECO:0000255"
FT REGION 702..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 966..970
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
FT COMPBIAS 708..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P49424"
FT ACT_SITE 316
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P49424"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49424"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49424"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49424"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P49424"
FT SITE 204
FT /note="Plays an important role in maintaining the position
FT of the catalytic nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P49424"
FT MOD_RES 969
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477"
SQ SEQUENCE 1002 AA; 106997 MW; E7063AA19CB6CC92 CRC64;
MKTTVTKLLA TVAAASTIFG MSTLPAFAAE GKSASNGNSV NISDVNATAE TRALFDKLKN
SGKGDLRFGQ QHATDENISS SASQGDVYET TGKYPAVFGW DAGLALRGAE KPGSGADKNA
NAKALAQNIT DADSKGAIVT LSAHWCNPGT GKDFNDTTAV ASELLPGGKY SGTFNKELDA
IAATAQRAKR SDGTLIPIIF RPLHENNGSW FWWGATHASA SEYKELYRYI VDYLRDVKDV
HNLLYAYSPG GVFNGDSTDY LATYPGDQWV DVLGYDEYDS DDSADDSSAW INTVVKDMKM
VSDQASQRGK IVALTEFGRS GDRKFKESGT GDKDTKFFSE LAEALAENVP STAYMMTWAN
FGGGGDNFQA YTSWKGSDGE ADFKAFADSN KNLMASKDNV DYSNAPAAAM QNGSARIVTP
VDGNRVTDTK VVVRVKTEGV KYSDLDLNSA IVTTDRGQNV KLKYSCNGYF TGILDLNAAG
INLDQSKLTL TPQVKTKDGK TLAAADGNGS VTVKLGAKPE QTVDNVEDFD SYDNEAELQS
VYSPSHSTKS NLTLVDSPED NGTKAGNIHY DFVSYPEYNG FQRSHTPKQD WSGFSKLNMF
LKADGSDHKF VVQVNAGGVT FEAYPKIDGT DGHVVSLNFG DADGNGGDFA PASWDTAHAG
MKLSQKLLSK VGSFALYIND NGGNRPKSGD LTLDSIKLDG KRDAYAPNTN PTPGNTAKAQ
SVDDFSGYSD DAAAQSAWGN RGHTEVLSLD EGPTDGSKAL RFKYDFSNGG WYDVAKYLDG
ANWSGESVLA FQVKGDGSGN AIGLQIGTSD GKYFLASVKL DFTGWKQIEI PLVDNANLTQ
SWPEDANKDN PMTEDDLASI KELVFASQQW NSESDGLDSS IADIKVEPAE NTSNEQTPKD
ESKTEVKADK EQEQSEDTSA DVTAQDPATC PISDEDSKGS TGNTTVTVKP TPDTKEPADN
TGKDGLSRTG SNIISAIAAV AVLLLGGCAV LIARKRKGGD IE
