BGH9A_BACO1
ID BGH9A_BACO1 Reviewed; 587 AA.
AC A7LXT3;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Xyloglucan-specific endo-beta-1,4-glucanase BoGH9A;
DE EC=3.2.1.151;
DE AltName: Full=Glycosyl hydrolase family protein 9A;
DE Short=BoGH9A;
DE Flags: Precursor;
GN ORFNames=BACOVA_02649;
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, PATHWAY, AND
RP DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: Catalyzes endohydrolysis of 1,4-beta-D-glucosidic linkages in
CC xyloglucan with retention of the beta-configuration of the glycosyl
CC residues in xyloglucan degradation. Cleaves the backbone of the 3 major
CC types of natural xyloglucans (seed galactoxyloglucan from tamarind
CC kernel, dicot fucogalactoxyloglucan from lettuce leaves, and
CC solanaceous arabinogalactoxyloglucan from tomato fruit), to produce
CC xyloglucan oligosaccharides. May be superfluous in xyloglucan
CC degradation compared to BoGH5A (AC A7LXT7), the other Xyloglucan-
CC specific endo-beta-1,4-glucanase. {ECO:0000269|PubMed:24463512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
CC Evidence={ECO:0000269|PubMed:24463512};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
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: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Cell outer membrane
CC localization is predicted by analogy with the archetypal sus locus.
CC {ECO:0000269|PubMed:24463512}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. No effect on growth.
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 9 (cellulase E) family.
CC {ECO:0000255|PROSITE-ProRule:PRU10140, ECO:0000305}.
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DR EMBL; AAXF02000049; EDO11440.1; -; Genomic_DNA.
DR RefSeq; WP_004298437.1; NZ_DS264579.1.
DR PDB; 6DHT; X-ray; 1.42 A; A=21-583.
DR PDBsum; 6DHT; -.
DR AlphaFoldDB; A7LXT3; -.
DR SMR; A7LXT3; -.
DR STRING; 411476.BACOVA_02649; -.
DR CAZy; GH9; Glycoside Hydrolase Family 9.
DR EnsemblBacteria; EDO11440; EDO11440; BACOVA_02649.
DR GeneID; 29452182; -.
DR eggNOG; COG3291; Bacteria.
DR HOGENOM; CLU_006010_2_1_10; -.
DR UniPathway; UPA01045; -.
DR Proteomes; UP000005475; Unassembled WGS sequence.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase 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 CDD; cd02850; E_set_Cellulase_N; 1.
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; IPR004197; Cellulase_Ig-like.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR033126; Glyco_hydro_9_Asp/Glu_AS.
DR InterPro; IPR018221; Glyco_hydro_9_His_AS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF02927; CelD_N; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS60032; GH9_1; 1.
DR PROSITE; PS00592; GH9_2; 1.
DR PROSITE; PS00698; GH9_3; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell outer membrane; Glycosidase;
KW Hydrolase; Lipoprotein; Membrane; Palmitate; Polysaccharide degradation;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 20..587
FT /note="Xyloglucan-specific endo-beta-1,4-glucanase BoGH9A"
FT /id="PRO_0000425895"
FT ACT_SITE 185
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10140"
FT ACT_SITE 511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10059"
FT ACT_SITE 553
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT ACT_SITE 562
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10060"
FT LIPID 20
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 20
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6DHT"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6DHT"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 190..206
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:6DHT"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:6DHT"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 279..295
FT /evidence="ECO:0007829|PDB:6DHT"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:6DHT"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 306..323
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 331..335
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 353..367
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 370..378
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 393..400
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 409..430
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 439..445
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 453..456
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 458..472
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 475..488
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:6DHT"
FT STRAND 503..505
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 513..517
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 547..549
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 558..561
FT /evidence="ECO:0007829|PDB:6DHT"
FT HELIX 565..581
FT /evidence="ECO:0007829|PDB:6DHT"
SQ SEQUENCE 587 AA; 65325 MW; 5B67EFD3E10410DD CRC64;
MKIVRYIALF GILSGLAVAC TPSTSVIPND AIRLNQLGYY PNQEKIAVVD SGKVEEFVIW
DAVSGEQVFV GKSLYTAKSA WSDKTRTTLD FSAVTTPGKY ILKVNGASVT FLIKDSVLSP
LADAALKSFY YQRTAMPIEE QYAGQWHRMA GHPDNHVLIH PSAASPDRPA GTIVSSSKGW
YDAGDYNKYI VNSGYSIGLM QSIYQLFLDY FSRQKINIPE SNNHTPDLLD EMQFNLDWML
TMQDPEDGGV YHKLTTPFFE GFVKPVDCKQ QRYVVQKSVT AALDFAAVMA QSSRLFASYE
EDYPGFSKRA LLAAEKAYAW AEKHPEAYYN QNLLNQKYQP AIATGEYGDT HADDEFFWAA
SELYFSTGKE IYREEAIKKA PQIYTAPGWG NTFALGIFAW LQPGRELNEA DRRFADSLKT
ELLKYADKVI EGAEQTPFHA PYGNDAKDFF WGCLAEKCMN QGVSLMYAYL QTGKDVYLTN
AYRNMDYILG RNATGFCYVT GLGTKSPKHP HHRLSASDDI EDPIPGFLVG GPNPGQQDGA
FYPTASPDES YVDTEDSYAS NEVAINWNAA LVALASSLDA LAVYSVK
