GH31A_BACO1
ID GH31A_BACO1 Reviewed; 954 AA.
AC A7LXT0;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Alpha-xylosidase BoGH31A;
DE EC=3.2.1.177;
DE AltName: Full=Glycosyl hydrolase family protein 31A;
DE Short=BoGH31A;
DE Flags: Precursor;
GN ORFNames=BACOVA_02646;
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 the liberation of alpha-xylose from the non-
CC reducing terminal glucose of xyloglucan oligosaccharides in xyloglucan
CC degradation, converting the 'X' to 'G' units.
CC {ECO:0000269|PubMed:24463512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-xylose residues
CC with release of alpha-D-xylose.; EC=3.2.1.177;
CC Evidence={ECO:0000269|PubMed:24463512};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.7 mM for Xyl-alpha-PNP {ECO:0000269|PubMed:24463512};
CC KM=31.8 mM for Glc-alpha-PNP {ECO:0000269|PubMed:24463512};
CC KM=0.223 mM for XXXG {ECO:0000269|PubMed:24463512};
CC KM=0.378 mM for XLLG {ECO:0000269|PubMed:24463512};
CC KM=38.1 mM for isoprimeverose {ECO:0000269|PubMed:24463512};
CC Note=kcat is 1.6 sec(-1) for Xyl-alpha-PNP. kcat is 0.071 sec(-1) for
CC Glc-alpha-PNP. kcat is 32.6 sec(-1) for XXXG. kcat is 31.0 sec(-1)
CC for XLLG. kcat is 1.78 sec(-1) for isoprimeverose.;
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 inner membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}. Note=Cell inner membrane
CC localization is predicted by analogy with the archetypal sus locus.
CC {ECO:0000269|PubMed:24463512}.
CC -!- DISRUPTION PHENOTYPE: Severely reduced growth on tamarind xyloglucan
CC and completely abolished growth on XyG oligosaccharides.
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 31 family. {ECO:0000305}.
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DR EMBL; AAXF02000049; EDO11437.1; -; Genomic_DNA.
DR PDB; 5JOU; X-ray; 1.50 A; A=22-954.
DR PDB; 5JOV; X-ray; 1.50 A; A=22-954.
DR PDBsum; 5JOU; -.
DR PDBsum; 5JOV; -.
DR AlphaFoldDB; A7LXT0; -.
DR SMR; A7LXT0; -.
DR STRING; 411476.BACOVA_02646; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR PRIDE; A7LXT0; -.
DR EnsemblBacteria; EDO11437; EDO11437; BACOVA_02646.
DR eggNOG; COG1501; Bacteria.
DR HOGENOM; CLU_000631_7_3_10; -.
DR SABIO-RK; A7LXT0; -.
DR UniPathway; UPA01045; -.
DR Proteomes; UP000005475; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0061634; F:alpha-D-xyloside xylohydrolase; IEA:UniProtKB-EC.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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; 2.60.40.1180; -; 2.
DR InterPro; IPR032513; AGL_N.
DR InterPro; IPR033403; DUF5110.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR000322; Glyco_hydro_31.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR037524; PA14/GLEYA.
DR Pfam; PF16338; DUF4968; 1.
DR Pfam; PF17137; DUF5110; 1.
DR Pfam; PF01055; Glyco_hydro_31; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR PROSITE; PS51820; PA14; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cell inner membrane; Cell membrane;
KW Glycosidase; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW Polysaccharide degradation; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..954
FT /note="Alpha-xylosidase BoGH31A"
FT /id="PRO_0000425896"
FT DOMAIN 227..366
FT /note="PA14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT ACT_SITE 553
FT /evidence="ECO:0000250"
FT ACT_SITE 556
FT /evidence="ECO:0000250"
FT ACT_SITE 630
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:5JOU"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 141..150
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:5JOU"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 273..284
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 296..302
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 333..340
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 363..380
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 384..395
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:5JOV"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 463..472
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 476..481
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 483..486
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 504..507
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 528..541
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:5JOU"
FT TURN 555..557
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 565..571
FT /evidence="ECO:0007829|PDB:5JOU"
FT TURN 580..582
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 587..602
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 619..622
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:5JOV"
FT HELIX 635..650
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 667..679
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 684..700
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 703..708
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 717..720
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 726..740
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 742..754
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 763..766
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 771..773
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:5JOU"
FT TURN 783..785
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 786..788
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 797..803
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 809..811
FT /evidence="ECO:0007829|PDB:5JOU"
FT TURN 812..814
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 820..827
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 835..838
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 842..845
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 859..865
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 870..876
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 879..882
FT /evidence="ECO:0007829|PDB:5JOU"
FT HELIX 883..886
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 890..897
FT /evidence="ECO:0007829|PDB:5JOU"
FT TURN 898..901
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 902..905
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 917..927
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 941..948
FT /evidence="ECO:0007829|PDB:5JOU"
FT STRAND 950..953
FT /evidence="ECO:0007829|PDB:5JOU"
SQ SEQUENCE 954 AA; 109785 MW; DA1FFF7BC54AFF75 CRC64;
MIMNMKNIFY CLLPGLLLGA CSNKVYEKTG DSVIVKVQHK ETGGPRLVRL QVMGDKLIHV
SATADSKFAD PQSLIVVPQK KQTSFAVVQN GDTITVSTEE VKASVLASTG EVWFTDKNGE
LILQENKGGG KTFTPIEVEG TKGYTVCQVF ESPEDEAFYG LGQHQADEFN YKGKNEELFQ
YNTKVSVPFV VSNKNYGILL DSYSFCRFGN PNDYSQLNRI FKLYDKTGQE GALTGTYVPK
KGETLVRRED SIYFENLKTI ENLPKKLPLM GAKVTYEGEI EPAQTGEFKF ILYYAGYVKV
YLNNEPVVPE RWRTAWNPNS YKFAAHLEAG KRVPLKIEWQ PDGGQSYCGL RALTPVNPEE
QGKQSWWSEM TKQLDYYFMA GENMDDVISG YRSLTGKSPV MPKWAMGFWQ SREKYNTQEE
MLGALKGFRD RKIPLDNIVL DWNHWPENAW GSHEFDKARF PDPKAMVDSI HAMHARMMIS
VWPKFYVTTE HFKEFDENGW MYQQSVKDSL KDWVGPGYHY GFYDAYDPDA RKLFWKQMYE
HYYPLGIDAW WMDASEPNVR DCTDLEYRKA LCGPTALGSS TEFFNAYALM NAEAIYDGQR
GVDNNKRVFL LTRSGFAGLQ RYSTATWSGD IGTRWEDMKA QISAGLNFAM SGIPYWTMDI
GGFCVENRYV AGQKQWNATK TENADYKEWR ELNTRWYQFG AFVPLYRAHG QYPFREIWEI
APEGHPAYQS VVYYTKLRYN MMPYIYSLAG MTWFDDYTIM RPLVMDFTAD AEVNDIGDQF
MFGPSFMVSP VYRYGDRSRE IYFPQAEGWY DFYSGKFQAG GERKVIEAPY ERIPLYVRAG
AIIPFGDDIQ YTDEKPAEHI RLYIYQGADG EFTLYEDEGV NYNYEQGMYA MIPMKYDEAT
KTLVIGERQG EFPGMLKERT FTVVTVNKEK AQPFDLNAKG VTVKYNGSEQ TLKL
