GH43B_BACO1
ID GH43B_BACO1 Reviewed; 529 AA.
AC A7LXU0;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Non-reducing end alpha-L-arabinofuranosidase BoGH43B;
DE EC=3.2.1.55;
DE AltName: Full=Glycosyl hydrolase family protein 43B;
DE Short=BoGH43B;
DE Flags: Precursor;
GN ORFNames=BACOVA_02656;
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 (2.28 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=6.6 mM for L- Araf-alpha-PNP {ECO:0000269|PubMed:24463512};
CC Note=kcat is 0.0005 sec(-1) for L- Araf-alpha-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDO11447.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AAXF02000049; EDO11447.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_052587925.1; NZ_DS264579.1.
DR PDB; 5JOZ; X-ray; 2.28 A; A/B=24-529.
DR PDBsum; 5JOZ; -.
DR AlphaFoldDB; A7LXU0; -.
DR SMR; A7LXU0; -.
DR STRING; 411476.BACOVA_02656; -.
DR EnsemblBacteria; EDO11447; EDO11447; BACOVA_02656.
DR GeneID; 29452223; -.
DR eggNOG; COG3507; Bacteria.
DR HOGENOM; CLU_016508_2_0_10; -.
DR SABIO-RK; A7LXU0; -.
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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..529
FT /note="Non-reducing end alpha-L-arabinofuranosidase
FT BoGH43B"
FT /id="PRO_0000425898"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:27466444"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:27466444"
FT SITE 148
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 26..29
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 57..71
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:5JOZ"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5JOZ"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 108..117
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:5JOZ"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 181..190
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:5JOZ"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 291..299
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:5JOZ"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:5JOZ"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 390..399
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 408..416
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 419..428
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 431..440
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 443..451
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 466..475
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 478..487
FT /evidence="ECO:0007829|PDB:5JOZ"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:5JOZ"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:5JOZ"
FT STRAND 518..527
FT /evidence="ECO:0007829|PDB:5JOZ"
SQ SEQUENCE 529 AA; 58620 MW; 59D13408E3FC858D CRC64;
MMKNSCRLLL ILIGLWMANV SLAQKTFRNP IITGMNPDPS ICRVGDDFYL VTSTFEYFPG
LPVYHSKDLV HWKLIGHALS RPENNPLMGC NASTGGQYAP TLRYHDGTFY VIGTNYGGKG
SQGVFYVTAK NPAGPWSDPV WVGNWYVDPS IEFIDGKMYF LSPDNQGSFL LGVMDPETGT
FVEALRKVAS GLGGSSPEGP HFYKIGDYYY IMSAEGGTGY EHREVIQRSK SPWGPYEPSP
VNPVLSNMNC PDHPFQAIGH ADLVQLKDGS WWAVCLGIRP VNGKYQHLGR ETFLAPVTWD
ADGWPKVGKD GVVQETYLFP NLPSHVWMEQ PVRDDFDQET LGLDWTFIRN PAHSFWSLTE
KPGSLRLKGT AINFTTNDSP SFIGRRQAAF NLTASAKVNF IPKVENEEAG LVVRADDKNH
YDLLITERNG QRVAMIRKTL KDKVVDTTCK ELPATGEVIL SITATETTYT FEIKAAHVSA
ILGTASTRDV SNEVVGGFTG VFIGMYASGN GQANTNPADF DWFDFRCLD
