EXGAL_BIFL2
ID EXGAL_BIFL2 Reviewed; 1513 AA.
AC A0A401ETL2;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Exo-beta-1,6-galactobiohydrolase {ECO:0000303|PubMed:30564851};
DE EC=3.2.1.213 {ECO:0000269|PubMed:30564851};
DE AltName: Full=Galactan exo-1,6-beta-galactobiohydrolase (non-reducing end) {ECO:0000305};
DE Flags: Precursor;
GN Name=bl1,6Gal {ECO:0000303|PubMed:30564851};
GN OrderedLocusNames=BLLJ_1841 {ECO:0000312|EMBL:BAJ67505.1};
OS Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM
OS 1217 / NCTC 11818 / E194b).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=565042;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=30564851; DOI=10.1007/s00253-018-9566-4;
RA Fujita K., Sakamoto A., Kaneko S., Kotake T., Tsumuraya Y., Kitahara K.;
RT "Degradative enzymes for type II arabinogalactan side chains in
RT Bifidobacterium longum subsp. longum.";
RL Appl. Microbiol. Biotechnol. 103:1299-1310(2019).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b;
RX PubMed=21270894; DOI=10.1038/nature09646;
RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T.,
RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J.,
RA Morita H., Hattori M., Ohno H.;
RT "Bifidobacteria can protect from enteropathogenic infection through
RT production of acetate.";
RL Nature 469:543-547(2011).
CC -!- FUNCTION: Involved in the type II arabinogalactan (AG) side chains
CC degradation (PubMed:30564851). Specifically releases the non-reducing
CC terminal beta-1,6-galactobiose (beta-1,6-Gal2) from both
CC dearabinosylated larch AG and polymeric beta-1,6-galactan chains by an
CC exo-mode of action (PubMed:30564851). Shows lower activity with larch
CC AG, and very weak activity with dearabinosylated gum arabic, gum arabic
CC and potato galactan (PubMed:30564851). Can probably release beta-1,6-
CC Gal2 from the internal side chains of type II AG (PubMed:30564851).
CC {ECO:0000269|PubMed:30564851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->6)-beta-D-galactosidic linkages in
CC arabinogalactan proteins and (1->3):(1->6)-beta-galactans to yield
CC (1->6)-beta-galactobiose as the final product.; EC=3.2.1.213;
CC Evidence={ECO:0000269|PubMed:30564851};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.549 mM for beta-1,6-Gal3 {ECO:0000269|PubMed:30564851};
CC Note=kcat is 261 sec(-1) with beta-1,6-Gal3 as substrate.
CC {ECO:0000269|PubMed:30564851};
CC pH dependence:
CC Optimum pH is 4.5 with beta-1,6-Gal3 as substrate.
CC {ECO:0000269|PubMed:30564851};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius with beta-1,6-Gal3 as
CC substrate. {ECO:0000269|PubMed:30564851};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 30 family. {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; BR001494; FAA01256.1; -; Genomic_DNA.
DR EMBL; AP010888; BAJ67505.1; -; Genomic_DNA.
DR RefSeq; WP_013583001.1; NZ_JGYZ01000008.1.
DR BioCyc; MetaCyc:MON-21026; -.
DR BRENDA; 3.2.1.145; 10148.
DR BRENDA; 3.2.1.213; 10148.
DR BRENDA; 3.2.1.55; 10148.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR039743; 6GAL.
DR InterPro; IPR011081; Big_4.
DR InterPro; IPR025883; Cadherin-like_b_sandwich.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR022038; Ig-like_bact.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR42767; PTHR42767; 1.
DR Pfam; PF07523; Big_3; 1.
DR Pfam; PF07532; Big_4; 1.
DR Pfam; PF12733; Cadherin-like; 1.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF14200; RicinB_lectin_2; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Glycosidase; Hydrolase; Membrane;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..1513
FT /note="Exo-beta-1,6-galactobiohydrolase"
FT /evidence="ECO:0000255"
FT /id="PRO_5019526962"
FT TRANSMEM 1489..1509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 666..801
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 965..1112
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 1116..1273
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 1456..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1513 AA; 159668 MW; C2686AF26A5093A0 CRC64;
MRVLSKSLAA MVAAATLVGG GAFAVAGTAY AADNDAITVT PNPWYANSFD GWGTSLAWFA
NATGSLGEES AITTNLGDDA SKAKAVEYGK QLREQFYQSI FGDEGLDLNM ARYNVGGGNA
SDVAYGYPFM RQGAAVPGTW KDDATGSGTY GNGVTTKQAD KDKLAAAFDP TDDNQYDFSK
SAAQDWWIER GATGDNPDIT DVEAFANSAP WFLTNSGYAT GGRNSGSNNL ANPEKFAQYM
AKNVEHLESL GANVDTVEPF NESETSYWGT PGDMASKYTD ESDDNTKLIN NYWDKYYSDK
DRSVTPYSNA LKKPQEGMHV SNAQQQQTIT ALAEALKDND DTIIAATDAT NSADFVKSYN
QYPQAIKDLI GQYNVHAYSD SNQMQSRDIA QADGKKLSMS EVDGSWQSGS YNPYGFDNAL
GMMSKISSNV TRLQSKDFTF WQVVEDLYNM QMGSNVNPAG ENTNWGTVLI DFDCTVAGMD
GKLYSERRVN NNGGTTDGLE PCTVIANAKY NGVKAITHFI HAGDKVIANN DEDNNMTATS
DDGKTQTVIH RNSGTSDQTF VIDLSKYGEI ADNAYGELYL TTETSAEDKN AGVDSATPEV
FAKTSNVKQA EGSVMIDKAA KTATVTVPAR SIASIQLTGV TGYAKDAAVE TGDTYQLVGK
QSGKAVADTT SGDSALSLAN VASDAENAKK QTWTFTQIEQ PTDSERPDLK AYVITNAEGK
VLVSKDGTNA LSNETVGAAK SDPAAKWILN TSDGSTYQLL NAATKTNLDV DNSGTTVGTK
VGLWQSPSGT SPSANQTWTL RNVTPTSQKT VNVQTAVNEK AVLPVEVTLY YTWGEGKATV
ANWDTSKVDV AKEGAYEATA TATDVYGNEF NVTATVYVGA LTVSDPVSAT VLAGTSASEA
KAALEAAPVY LHVKASPAFE GDAAKVTWNF DGLDTKLADA KAGDNIAVTG TYQLDDATTI
ALKGAIYVTA ATPENVADTA SNLTVTNQQT EYSKGDQWKK LTDGDTSAEA WVTWNSAGDY
SASPTATIDF GSECELSSVT ITYGDKAPAS AKAEYTTDGE TWMQFGSDVK PAAGQTVTFK
ADKGTVNATK MRIVNTVNND YMNATEIQAF VTPVQGAAKN IAAASGTNFS VNFQEGASAS
KAIDGDTTSK GWSTWASTAS TVDPVATFTF DEAQTITEVK TFFYYDGRAS WPKSQTLEYQ
DEAGEWHGVG TKDGWKIQAG DAGSGSDGIT AADTPTVDFV LGTPVKAKAI RLTNTLQDTK
VYINVAEIQV FAQDSTVLTP QPASDATLGD LRLDGETVEG FDPSKTDYTV DLPVDAEANP
VLQAFATDNA AAVKVTGDAV ENGKLGGKAA ITVTSADESE TKTYTVTFNA FTLASLKVIG
PTKTEYAIGD KLDTAGLKVT AVYQSGDKTK EVPVALDDPQ LAIGSFDSTT AGKKAITVSY
RGVTATFNVT VKANAVAPGP EEQKPGNTNK PGATGNGNKN TVANTGSSVA AIAGAVALLA
AAAGALFMLR KRA
