HYBA2_BIFL2
ID HYBA2_BIFL2 Reviewed; 1943 AA.
AC E8MGH9; E7FK76;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Beta-L-arabinobiosidase;
DE EC=3.2.1.187;
DE AltName: Full=Arabinofuranosyl(3)-Hyp beta-L-arabinobiosidase;
DE Flags: Precursor;
GN Name=hypBA2; OrderedLocusNames=BLLJ_0212;
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=21149454; DOI=10.1074/jbc.m110.190512;
RA Fujita K., Sakamoto S., Ono Y., Wakao M., Suda Y., Kitahara K.,
RA Suganuma T.;
RT "Molecular cloning and characterization of a beta-L-arabinobiosidase in
RT Bifidobacterium longum that belongs to a novel glycoside hydrolase
RT family.";
RL J. Biol. Chem. 286:5143-5150(2011).
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: Beta-L-arabinobiosidase that removes L-arabinofuranose-beta-
CC 1,2-L-arabinofuranose disaccharide from various substrates such as
CC carrot extensin and potato lectin. Also acts on L-arabinofuranose
CC (Ara)-beta-1,2-Ara-beta-1,2-Ara-beta-Hyp (Ara(3)-Hyp) but not on Ara-
CC beta-1,3-Ara-beta-1,2-Ara-beta-1,2-Ara-beta--Hyp (Ara(4)-Hyp) or Ara-
CC beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), suggesting a specificity for
CC unmodified Ara(3)-Hyp substrate. In the presence of 1-alkanols, shows
CC transglycosylation activity, retaining the anomeric configuration of
CC the arabinofuranose residue. {ECO:0000269|PubMed:21149454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-O-(beta-L-arabinofuranosyl-(1->2)-beta-L-arabinofuranosyl-
CC (1->2)-beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + H2O = 4-O-
CC (beta-L-arabinofuranosyl)-(2S,4S)-4-hydroxyproline + beta-L-
CC arabinofuranosyl-(1->2)-beta-L-arabinofuranose; Xref=Rhea:RHEA:38447,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:73180, ChEBI:CHEBI:75879,
CC ChEBI:CHEBI:75880; EC=3.2.1.187;
CC Evidence={ECO:0000269|PubMed:21149454};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:21149454};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:21149454};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 121 family.
CC {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; AB562506; BAJ34647.1; -; Genomic_DNA.
DR EMBL; AP010888; BAJ65882.1; -; Genomic_DNA.
DR RefSeq; WP_013582352.1; NC_015067.1.
DR PDB; 6M5A; X-ray; 1.85 A; A=33-894.
DR PDBsum; 6M5A; -.
DR AlphaFoldDB; E8MGH9; -.
DR SMR; E8MGH9; -.
DR CAZy; GH121; Glycoside Hydrolase Family 121.
DR KEGG; blm:BLLJ_0212; -.
DR HOGENOM; CLU_002496_0_0_11; -.
DR OMA; SWIHHTQ; -.
DR BioCyc; MetaCyc:MON-18165; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR011081; Big_4.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF07532; Big_4; 2.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF49785; SSF49785; 2.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; Membrane;
KW Polysaccharide degradation; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..32
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 33..1943
FT /note="Beta-L-arabinobiosidase"
FT /id="PRO_0000423556"
FT TRANSMEM 1908..1928
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 892..1049
FT /note="F5/8 type C 1"
FT DOMAIN 1061..1157
FT /note="PKD"
FT DOMAIN 1142..1302
FT /note="F5/8 type C 2"
FT DOMAIN 1678..1716
FT /note="FIVAR 1"
FT DOMAIN 1746..1790
FT /note="FIVAR 2"
FT DOMAIN 1823..1864
FT /note="FIVAR 3"
FT REGION 1875..1906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:6M5A"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 210..222
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 322..340
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 349..364
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:6M5A"
FT TURN 385..388
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 393..403
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 410..421
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 451..462
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 466..484
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 492..494
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 534..554
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 557..577
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:6M5A"
FT TURN 581..584
FT /evidence="ECO:0007829|PDB:6M5A"
FT TURN 591..593
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 602..605
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 606..609
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 618..622
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 623..628
FT /evidence="ECO:0007829|PDB:6M5A"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 643..648
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 659..675
FT /evidence="ECO:0007829|PDB:6M5A"
FT TURN 678..682
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 686..700
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 702..704
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 728..730
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 733..740
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 763..767
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 776..778
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 792..800
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 803..810
FT /evidence="ECO:0007829|PDB:6M5A"
FT TURN 814..816
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 820..826
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 829..836
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 840..843
FT /evidence="ECO:0007829|PDB:6M5A"
FT TURN 844..847
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 848..851
FT /evidence="ECO:0007829|PDB:6M5A"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 872..874
FT /evidence="ECO:0007829|PDB:6M5A"
FT HELIX 883..887
FT /evidence="ECO:0007829|PDB:6M5A"
SQ SEQUENCE 1943 AA; 210438 MW; E5193BD671F72CAB CRC64;
MHHSTRKRWL ASIGAVAAVA TLATGGAVTA QAADAPVIKN ADVAYPSFKG SDDPMKTAAN
NTTYNPAVSY LQETFDNDVK NLAGIDTDHD FWIDKILTRT GAQPTGKGTN DKGAYSYEGS
DGNNYLFTRG RAAYMYTHTP NQLGFVGDTA YWDQTSRSGF TVTVNADGSN QTLNEDASQR
KQTPSYFTSL FQTGGKSLKI KEVKYITYNN VMVANLTVES TQDRDVTLTT ASPFAAEGAD
GATELTGRVN VKNNLTTIYP RFSANNQDGS NWIVSGGKLT STLSLKANEP QTVKIQLGLI
ANELPDSTKE YEARYTGDLK DAAASYKDSV TTYNKWWVDN APYVDTPEDN IDKTVVYRWW
LSRFNMLDAN MPGNTFQYPT SIEGVLGYNN QIVLTSGMFM MDTKWFRNPE YSYGTWLSAG
DTAKKSKAGY YYYHDNPGDP ANWNHSYTQY ITRAGWDSYK VHGGPSTVAE ELADQGAEDV
QGLLASKSEP DNNDNQNNND NSLIDWSWWS MTGNDADAVS FSEPGRSGQR MDRADGSANM
WANANAAAQA YKAAGDTANA EKMQAIADKI QKEVTTELWD KSDNLLKHKW LNDGAFAKYK
EINNYYPYSE GLMPTGNEDY NKALRLFEDS NEFPIFPFFT ANQADKAALN FPGSNNFSII
NAQPLLQVYS AGIRNYDAAK NGYITNEQFK KLLYWVAFAH YQGGDNNYPD QNEFWNEDNN
NVGDVNGDGV INNLDKNLDA AQNGGKITYR SWIHHTQLGT TNWTMVEDVA GMVPREDNKI
ELNPIEIPGW NYFTVNNLRY HDQDVSIVWD KDGSHYGGPA GYSLYVGGKL AFTSDKLAHL
IYDPAAGTVE VKDDSSAQVT VGAEAVKNVK AANQVTFNAD QRVTDLFAKS GTNVDSASKS
TTNVAKDADV TGTTYAEKDT NYPAKNAVDG KTVMESFWGT KGSENKTDTL NIKFKDGKQK
IDDIRLYFYQ SSSSQTISGY AEPANYKLEY QKDDGTWAPI ADQVRTPNYA GANYNRIQFT
PVETTTIRVT FTPQAGMAVG VKEIEAYNTG IKADGTSENQ TPQVDAYVSS STSSGAKLVG
TVKDDGLPAE GDVTTTWSQV SGPEGGTAKF VDASAASTTV TFNKEGDYVL KLTASDGEKE
GSKEITVHGI PSDGTVNVAP QSSASASYTN GYQPKDNAKK VIDGQVVYAN TPNETWNNWG
DSTGVEPWLQ LKWAGKVPLK KAKVFFWTDG GGVPMVSSWK LQYADADGNW QDVKLADGQS
YTVNRNEGNE VKFADAVETD KLRVVFPKGA IVGASEFEAY AIEPVSVDEV NRLVQTGSKA
DDLKLPSTVS AVYTDGSRRD LAVTWGKVTD AQLAADAVFD VKGTVAGALN GTVAHIAARS
DTASQTVGNA QPVEQTVYQN AKSIDLPATV PVKFPNGYND DRKVTWKDAD IKAIDLTKVG
DYEVAGTVDD GSSSAAAKLT VHVVADPNGS STPEPEPEPL VGWIEGKATR TTISPDSEAT
WSPAEGKLND GVVVDDTWPT TDDQNVNDKV WGSWGKAKDG MYAQYDFGQS VTIDQSRAQF
WANFAETDDS KGGLEVPDAW KIQYLAEDGS WKDVEPTEDY TVVRNSPASR ADTDAKGWSA
VTFKPVTTKS LRLVLTPYTG SSTFGAAVAE WGVHGIDGTE PEPTPVDKTA LESALDTANG
LDASRYTAAS WAEFQQIIDA AQAVYDDANA TAEQVAEQVT KLEDGQKALV ALATDVEKST
LQAAIDAAKA EAASGKYTDK SVEALNKAIE AAEGVLKVGE VGEVTQAAVQ EASASLNKAV
KALEEKPAAE TVKKESLEAS IEQAKKADKS KYTEEAWQAL QSQIAAAQKV YDDKDAKQAD
VDAAQDALDK AFWATKVEQK PGSQQPGVTD TDKDDKDNKG DRVPPTGAAV SVVAAAAVLL
TAAGVTILKR RQSGDHGSAR HSA
