GH43A_BACO1
ID GH43A_BACO1 Reviewed; 526 AA.
AC A7LXT8;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Non-reducing end alpha-L-arabinofuranosidase BoGH43A;
DE EC=3.2.1.55;
DE AltName: Full=Glycosyl hydrolase family protein 43A;
DE Short=BoGH43A;
DE Flags: Precursor;
GN ORFNames=BACOVA_02654;
OS Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 /
OS CCUG 4943 / NCTC 11153).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=411476;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC
RC 11153;
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides ovatus (ATCC 8483).";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=24463512; DOI=10.1038/nature12907;
RA Larsbrink J., Rogers T.E., Hemsworth G.R., McKee L.S., Tauzin A.S.,
RA Spadiut O., Klinter S., Pudlo N.A., Urs K., Koropatkin N.M., Creagh A.L.,
RA Haynes C.A., Kelly A.G., Cederholm S.N., Davies G.J., Martens E.C.,
RA Brumer H.;
RT "A discrete genetic locus confers xyloglucan metabolism in select human gut
RT Bacteroidetes.";
RL Nature 506:498-502(2014).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS).
RX PubMed=27466444; DOI=10.1098/rsob.160142;
RA Hemsworth G.R., Thompson A.J., Stepper J., Sobala L.F., Coyle T.,
RA Larsbrink J., Spadiut O., Goddard-Borger E.D., Stubbs K.A., Brumer H.,
RA Davies G.J.;
RT "Structural dissection of a complex Bacteroides ovatus gene locus
RT conferring xyloglucan metabolism in the human gut.";
RL Open Biol. 6:160142-160142(2016).
CC -!- FUNCTION: Alpha-L-arabinofuranosidase involved in xyloglucan
CC degradation by mediating the cleavage of terminal non-reducing alpha-L-
CC arabinofuranoside residues in xyloglucan branches, converting the 'S'
CC units to 'X' units. {ECO:0000269|PubMed:24463512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC Evidence={ECO:0000269|PubMed:24463512};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.71 mM for L-Araf-alpha-PNP {ECO:0000269|PubMed:24463512};
CC KM=6.58 mM for Xyl-beta-PNP {ECO:0000269|PubMed:24463512};
CC Note=kcat is 0.057 sec(-1) for L-Araf-alpha-PNP. kcat is 0.26 sec(-1)
CC for Xyl-beta-PNP.;
CC pH dependence:
CC Optimum pH is 6.0-7.0. {ECO:0000269|PubMed:24463512};
CC -!- PATHWAY: Glucan metabolism; xyloglucan degradation.
CC {ECO:0000269|PubMed:24463512}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. Note=Periplasmic
CC localization is predicted by analogy with the archetypal sus locus.
CC {ECO:0000269|PubMed:24463512}.
CC -!- MISCELLANEOUS: Gut bacteria supply the human body with energy from
CC dietary polysaccharides through glycosidases that are absent in the
CC human genome. Xyloglucans are a ubiquitous family of highly branched
CC plant cell wall polysaccharides present in the vegetables we consume.
CC Enzymes involved in xyloglucan degradation mediate the conversion of
CC otherwise indigestible plant polysaccharides to short-chain fatty acids
CC (PubMed:24463512). {ECO:0000305|PubMed:24463512}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR EMBL; AAXF02000049; EDO11445.1; -; Genomic_DNA.
DR RefSeq; WP_004298447.1; NZ_DS264579.1.
DR PDB; 5JOW; X-ray; 1.60 A; A/B=21-526.
DR PDB; 5JOX; X-ray; 1.80 A; A/B=21-526.
DR PDB; 5JOY; X-ray; 1.90 A; A/B=21-526.
DR PDBsum; 5JOW; -.
DR PDBsum; 5JOX; -.
DR PDBsum; 5JOY; -.
DR AlphaFoldDB; A7LXT8; -.
DR SMR; A7LXT8; -.
DR STRING; 411476.BACOVA_02654; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR EnsemblBacteria; EDO11445; EDO11445; BACOVA_02654.
DR GeneID; 29452222; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_016508_2_0_10; -.
DR SABIO-RK; A7LXT8; -.
DR UniPathway; UPA01045; -.
DR Proteomes; UP000005475; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IDA:UniProtKB.
DR GO; GO:0085030; P:symbiotic process benefiting host; IDA:UniProtKB.
DR GO; GO:2000899; P:xyloglucan catabolic process; IDA:UniProtKB.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycosidase; Hydrolase; Periplasm;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..526
FT /note="Non-reducing end alpha-L-arabinofuranosidase
FT BoGH43A"
FT /id="PRO_0000425897"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:27466444"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:27466444"
FT SITE 140
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000305|PubMed:27466444"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 53..67
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5JOW"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:5JOW"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:5JOW"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:5JOW"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:5JOW"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 247..258
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:5JOW"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:5JOW"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:5JOW"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 357..360
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 382..394
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 400..408
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 411..419
FT /evidence="ECO:0007829|PDB:5JOW"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 425..433
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 436..444
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:5JOX"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 459..468
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 471..479
FT /evidence="ECO:0007829|PDB:5JOW"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:5JOW"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:5JOW"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:5JOW"
SQ SEQUENCE 526 AA; 58966 MW; 190EBA9760F7400F CRC64;
MRNALFLIFI SLCSVCKSSA QGYSNPVIPG FHPDPSVCKA GDDYYLVNSS FQYFPGVPLF
HSKDLVHWEQ IGNCLTRPSQ LDLTNANSGS GIFAPTIRYN DGVFYMITTN VSGKGNFLVH
TTDPRSEWSE PVWLEQGGID PSLYFEDGKC FMVSNPDGYI NLCEIDPMTG KQLSSSKRIW
NGTGGRYAEG PHIYKKDGWY YLLISEGGTE LGHKVTIARS RYIDGPYQGN PANPILTHAN
ESGQSSPIQG TGHADLVEGT DGSWWMVCLA YRIMPGTHHT LGRETYLAPV RWDKDAWPVV
NSNGTISLKM DVPTLPQQEM KGRPERIDFK EGKLSPEWIH LQNPEAKNYI FTKDGKLRLI
ATPVTLSDWK SPTFVALRQE HFDMEASAPV VLQKAGVNDE AGISVFMEFH SHYDLFVRQD
KDRKRSVGLR YKLGEITHYA KEVSLPTDGE VELVVKSDIN YYYFGYKVNG IYHDLGKMNT
RYLSTETAGG FTGVVLGLYI TSASKDSKAY ADFEYFKYKG KPGENK
