ID A0A2M9HB10_9BIFI Unreviewed; 895 AA.
AC A0A2M9HB10;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 28-JAN-2026, entry version 28.
DE SubName: Full=Glycosyl hydrolase family 43 {ECO:0000313|EMBL:PJM74003.1};
GN ORFNames=CS006_02315 {ECO:0000313|EMBL:PJM74003.1};
OS Bifidobacterium primatium.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=2045438 {ECO:0000313|EMBL:PJM74003.1, ECO:0000313|Proteomes:UP000229095};
RN [1] {ECO:0000313|EMBL:PJM74003.1, ECO:0000313|Proteomes:UP000229095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRE1 {ECO:0000313|Proteomes:UP000229095};
RA Mattarelli P., Modesto M., Puglisi E., Morelli L., Spezio C., Bonetti A.,
RA Sandri C.;
RT "Draft genome sequences of strains TRE 1, TRE 9, TRE H and TRI 7, isolated
RT from tamarins, belonging to four potential novel Bifidobacterium species.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family.
CC {ECO:0000256|ARBA:ARBA00009865}.
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:PJM74003.1}.
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DR EMBL; PEBI01000001; PJM74003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9HB10; -.
DR OrthoDB; 9758923at2; -.
DR Proteomes; UP000229095; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd09003; GH43_XynD-like; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR005084; CBM6.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR InterPro; IPR052176; Glycosyl_Hydrlase_43_Enz.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR PANTHER; PTHR43772; ENDO-1,4-BETA-XYLANASE; 1.
DR PANTHER; PTHR43772:SF2; PUTATIVE (AFU_ORTHOLOGUE AFUA_2G04480)-RELATED; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SMART; SM00635; BID_2; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS51175; CBM6; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PJM74003.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00022651};
KW Reference proteome {ECO:0000313|Proteomes:UP000229095};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Xylan degradation {ECO:0000256|ARBA:ARBA00022651}.
FT TRANSMEM 869..889
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 572..707
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 804..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 895 AA; 93424 MW; 8878C1A8E03E2F42 CRC64;
MEHIGSRGIH RISARTVVSA FSAVICLVAV MMPMGAETAS AADGGAVNLI VNGDFENDTA
SWKSGTVWDA SKSTITAVSD DVHGGSKALK VTDRKSTDAG AIQSLNGKVT KGESYTGSMW
IKSTEDATFN FTICSGNGSG CGQIASAAVK AGAWTEIKGT AALGGNGDYS NPSLVIETVY
GTGKTGDFIV DDVTLTGKTS EPVVRPAGTA KAAKQVGNSN PIIDYWYGAD PWAMEYNGRV
YVYTTGDATK INEDGSLTYD YEYDADGNIK DNSFADVKTI NVLSTDDMVN WRNEGYIRVA
GDQGIAKWAG NSWAPAVTHK TIDGKEKFFL YFANGASGIG VLTADSPVGP WKDERGSLLI
KWGTQASSGV TWLFDPAVFT DSDGTGYLYY GGGVPDGQKE HPNTARVIQL GDDMISTVGD
AKTIDAPAMF EDSGIAKIGD TYYYSYCTNF SHENVIDGNK IGYGNIAYMT SKSPMGPFTY
QGEIMDNPSK FFSVGGNNHH AMVQLGNSWY MVYHAQTVAK ELTDGGNLDK ARGYRNTHVD
PITINKDGSI APITMTYKGL DQVKNLDAYP EGGISASTIA WDSGIQDAYD TKSGVRVIDL
TSDNADGQKL GNINDGEWTS LANVDFGKAG AKSITVNAAA KVGGNIEVRL DSNDTEPVAT
VKIPAGDGSA YADYTAALSG VTGVHNVFFT FKATQADKSN PELFDIKTYT FAKADPEPTV
VPVSGVSVSL ERDAVKVGES VLAKASVSPE NVSDKSVSWS SSDEKVAKVD ASGRVTAVGA
GAATITATAK DGSGVSGFAK LTVSADSSEK PGSGEGSSDK PSQNPSDGTG NNAGGGNSGK
TPSATISGVD NTSRRQVSNG SLARTGTSVA GIFGIAVVLV AVGVVLAICR KRCLS
//
