KEGG   ENZYME: 3.2.1.177Help
Entry
EC 3.2.1.177                Enzyme                                 

Name
alpha-D-xyloside xylohydrolase;
alpha-xylosidase
Class
Hydrolases;
Glycosylases;
Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
BRITE hierarchy
Sysname
alpha-D-xyloside xylohydrolase
Reaction(IUBMB)
Hydrolysis of terminal, non-reducing alpha-D-xylose residues with release of alpha-D-xylose.
Comment
The enzyme catalyses hydrolysis of a terminal, unsubstituted xyloside at the extreme reducing end of a xylogluco-oligosaccharide. Representative alpha-xylosidases from glycoside hydrolase family 31 utilize a two-step (double-displacement) mechanism involving a covalent glycosyl-enzyme intermediate, and retain the anomeric configuration of the product.
History
EC 3.2.1.177 created 2011
Orthology
K01811  alpha-D-xyloside xylohydrolase
K15925  alpha-D-xyloside xylohydrolase
Genes
ATH: AT1G68560(XYL1)
ALY: ARALYDRAFT_664955 ARALYDRAFT_894626
CRB: 17894865
CSAT: 104701486 104701487 104711051 104750674 104787899 104790831 109133314
EUS: EUTSA_v10018090mg
BRP: 103829450 103830964 103831266
BNA: 106353849 106355929 106371119 106394132 106403520 106405609 106410923 106442523
BOE: 106300147 106300429 106327168
THJ: 104821941
CPAP: 110824054
CIT: 102611225
TCC: 18610494
EGR: 104453802
VRA: 106753219
VAR: 108334917
CAM: 101494739
LJA: Lj0g3v0131439.1(Lj0g3v0131439.1) Lj0g3v0152159.1(Lj0g3v0152159.1) Lj2g3v1155320.1(Lj2g3v1155320.1) Lj2g3v1155420.1(Lj2g3v1155420.1)
FVE: 101294848
PPER: 18791156
PMUM: 103341474
PAVI: 110757163
ZJU: 107429422
RCU: 8285792
JCU: 105642021
VVI: 100262991
SOT: 102596982 102602461(MAL2)
INI: 109175993
BVG: 104896510
SOE: 110783462
OSA: 4325976
DOSA: Os01t0130400-01(Os01g0130400)
OBR: 102721487
BDI: 100830622
ATS: 109757376(LOC109757376)
SBI: 8073357
ZMA: 100501905
SITA: 101757308
PDA: 103712910
EGU: 105041200
MUS: 103992152
DCT: 110101364
AOF: 109829165
PIC: PICST_32530(YIC1)
SPAA: SPAPADRAFT_66805(YIC1)
MBE: MBM_05264
ANG: ANI_1_1306084(An09g03300) ANI_1_620014(An01g04880)
ZTR: MYCGRDRAFT_54143(MgAGL2)
ABP: AGABI1DRAFT121418(AGABI1DRAFT_121418)
ABV: AGABI2DRAFT75421(AGABI2DRAFT_75421)
ECO: b3656(yicI)
ECJ: JW3631(yicI)
ECD: ECDH10B_3838(yicI)
EBW: BWG_3347(yicI)
ECOK: ECMDS42_3090(yicI)
ECE: Z5084(yicI)
ECS: ECs4532
ECF: ECH74115_5029(yicI)
ETW: ECSP_4651(yicI)
EOJ: ECO26_4943(yicI)
EOI: ECO111_4479(yicI)
EOH: ECO103_4501(yicI)
ECOO: ECRM13514_4666(yicI)
ECOH: ECRM13516_4446(yicI)
ECG: E2348C_3928(yicI)
EOK: G2583_4393(yicI)
ESO: O3O_25110
ESM: O3M_00590
ESL: O3K_00560
ECW: EcE24377A_4160(yicI)
ELH: ETEC_3897
ECC: c4489(yicI)
ECP: ECP_3762
ECI: UTI89_C4209(yicI)
ECV: APECO1_2797(yicI)
ECX: EcHS_A3867(yicI)
ECY: ECSE_3939
ECR: ECIAI1_3830(yicI)
ECQ: ECED1_4349(yicI)
ECK: EC55989_4123(yicI)
ECT: ECIAI39_4186(yicI)
EOC: CE10_4224(yicI)
ECZ: ECS88_4080(yicI)
EBR: ECB_03514(yicI)
EBD: ECBD_0068
EKF: KO11_04415(yicI)
EAB: ECABU_c41230(yicI)
EDJ: ECDH1ME8569_3541(yicI)
EIH: ECOK1_4106(yicI)
ELW: ECW_m3933(yicI)
ELL: WFL_19225(yicI)
ELC: i14_4152(yicI)
ELD: i02_4152(yicI)
ELP: P12B_c3786(yicI)
EBL: ECD_03514(yicI)
EBE: B21_03466(yicI)
ELF: LF82_3357(yicI)
ECOI: ECOPMV1_03998(yicI)
ECOS: EC958_0154 EC958_4071(yicI)
EFE: EFER_3949(yicI)
STT: t0043 t3770
STM: STM0041 STM3749(yicI)
SPT: SPA0042
SEK: SSPA0038
SEI: SPC_0043
SEC: SCH_0036 SCH_3673(yicI)
SEG: SG0044 SG3683(yicI)
SEL: SPUL_0044 SPUL_3815(yicI)
SET: SEN0041 SEN3570(yicI)
SBG: SBG_3329
SBZ: A464_3826
SFL: SF3696(yicI)
SFX: S4073(yicI)
SFV: SFV_3873(yicI)
SFE: SFxv_4024(yicI)
SFN: SFy_5265
SFS: SFyv_5340
SFT: NCTC1_03990(yicI)
SBO: SBO_3721(yicI)
SBC: SbBS512_E4107(yicI)
ENC: ECL_00104
EEC: EcWSU1_00084(yicI)
ECLZ: LI64_00600
ENF: AKI40_0094(yicI)
ESA: ESA_04154
CSK: ES15_0125(yicI)
CTU: CTU_40820(yicI)
KPN: KPN_04018(yicI)
KPU: KP1_5378(yicI)
KPP: A79E_0095
KPE: KPK_0078(yicI)
KPR: KPR_0338
KPJ: N559_0127
KPX: PMK1_01522(yicI_1)
KPNU: LI86_00470
KPNK: BN49_0089
KVA: Kvar_0083
KOX: KOX_06150
KOE: A225_5700
EAE: EAE_06545
EAR: CCG32684
CAMA: F384_19870
EBF: D782_0057
EBI: EbC_00520
XCC: XCC1755(xylS)
XCB: XC_2480
XCA: xcc-b100_2507(aglA2)
XCP: XCR_1995
XCV: XCV1805
XAX: XACM_1796
XAC: XAC1773(xylS)
XFU: XFF4834R_chr27390(xylS)
XOO: XOO2914(xylS)
XOM: XOO2765(XOO2765)
XOP: PXO_00115
XAL: XALC_1194
XPH: XppCFBP6546_19170(XppCFBP6546P_19170)
PSUW: WQ53_13355
PAT: Patl_2861
PEA: PESP_a3824(yicI)
AMAC: MASE_18025
GPS: C427_1742
CJA: CJA_2706(xyl31A) CJA_2872(agd31A)
SDE: Sde_2500(xyl31A)
FTL: FTL_1054
TEA: KUI_1288
TEG: KUK_0736
TAS: TASI_1269
TAT: KUM_0630
PUT: PT7_0027
AMIM: MIM_c09890
AFQ: AFA_03755
DOL: Dole_1145
CCR: CC_0789
SPHR: BSY17_3127
BLI: BL02681
BLD: BLi03543
BCL: ABC1132
BGY: BGLY_3933
LWE: lwe0241
LSG: lse_2611
PPY: PPE_01798
PPM: PPSC2_09420(gaa)
PPO: PPM_1796(gaa)
PPOL: X809_09735
PPOY: RE92_02875
AAC: Aaci_2887
AAD: TC41_3242(yicI)
SSUI: T15_0591(yicI) T15_0592
LJO: LJ_0737
LAC: LBA1365
LAD: LA14_1363
LAF: SD55_1348
LBR: LVIS_0462
LGA: LGAS_0520
PPE: PEPE_0184
PPEN: T256_01040
EFA: EF0551
EFL: EF62_0923
EFN: DENG_00575(yicI)
EFQ: DR75_2509
ECAS: ECBG_02610
EMU: EMQU_0052
LME: LEUM_1244
WKO: WKK_04455
CAC: CA_C1085
CAE: SMB_G1103(yicI)
CSD: Clst_1171
ESR: ES1_02270
ESU: EUS_20290
CCEL: CCDG5_2026(yicI)
RCH: RUM_03990
RUM: CK1_36880
BPB: bpr_I1018(gh31A) bpr_I1974(gh31C)
ROB: CK5_13430
CPY: Cphy_0218
PDC: CDIF630_03354(xylS)
SAY: TPY_3224(yicI)
CSC: Csac_1354
ATE: Athe_2057
TSH: Tsac_1277
PFT: JBW_04509
LPIL: LIP_0426
MMY: MSC_0162(xylS)
MMYM: MMS_A0188
MMYI: mycmycITA_00182(yicI)
MML: MLC_1450(xylS)
MCP: MCAP_0156
MCAP: MCCPF38_00186(yicI)
MCAR: MCCPILRI181_00183(yicI)
MCAI: MCCG_0182
MLC: MSB_A0206
MPF: MPUT_0096
MPUT: MPUT9231_6450(xylS)
MFL: Mfl317
SLL: SLITO_v1c06090(yicI)
SHJ: SHELI_v1c09780(xylS)
SCO: SCO1055(SCG20A.35c)
SHY: SHJG_7999
SVE: SVEN_6629
SAMB: SAM23877_1146(yicI)
SPRI: SPRI_6751
SRW: TUE45_pSRc_0277(yicI)
SLE: sle_19900(sle_19900) sle_60510(sle_60510)
SRN: A4G23_00915(yicI_2)
STRD: NI25_33905
SMAL: SMALA_3057
CMI: CMM_0106(aglA) CMM_0362
BCV: Bcav_1323
JDE: Jden_1763
XCE: Xcel_1194
IDO: I598_0687(yicI_1) I598_3449(yicI_2)
CFI: Celf_2784
ACIJ: JS278_00495(yicI)
MPH: MLP_21570
KFL: Kfla_1824
TFU: Tfu_1613
NDA: Ndas_4927
SRO: Sros_1288
NML: Namu_0187
KRA: Krad_0413
AMD: AMED_4343(yicI)
AMN: RAM_22115
AMM: AMES_4290(yicI)
AMZ: B737_4290(yicI)
AMI: Amir_2986
ACTI: UA75_07325
ACAD: UA74_07330
AHG: AHOG_07040(yicI)
MIL: ML5_5249
ASE: ACPL_2433(yic1)
ACTN: L083_4105(yic1)
AFS: AFR_22430
ACTS: ACWT_2306
TPYO: X956_09040
BLJ: BLD_0073
BLF: BLIF_1434
BLL: BLJ_1317
BLM: BLLJ_1389
BLG: BIL_01020
BDE: BDP_1053 BDP_2149(aglL) BDP_2158(agl1)
BAST: BAST_1604
BCOR: BCOR_0873
BPSP: AH67_08265
BANG: BBAG_1558
BPSC: BBPC_1503
TBI: Tbis_2416
RXY: Rxyl_0705
HAU: Haur_1246
PBAS: SMSP2_01679(yicI_1) SMSP2_01681(yicI_2)
PBP: STSP1_00405(yicI_2) STSP1_01108(yicI_3)
VBL: L21SP4_00780(yicI)
ACA: ACP_1639(xylS2)
SUS: Acid_1796
ABAC: LuPra_02643(yicI)
BTHO: Btheta7330_00034(yicI_2) Btheta7330_03039(yicI_3) Btheta7330_04628(yicI_4)
BOA: Bovatus_00197(yicI_1) Bovatus_02519(yicI_2) Bovatus_02521(yicI_3) Bovatus_02568(yicI_4) Bovatus_03066(yicI_5) Bovatus_03718(yicI_7) Bovatus_03778(yicI_8) Bovatus_03899(yicI_9)
BCEL: BcellWH2_01207(yicI_1) BcellWH2_02281(yicI_2) BcellWH2_02842(yicI_4) BcellWH2_02846(yicI_5) BcellWH2_03181(yicI_6) BcellWH2_03346(yicI_7) BcellWH2_04220(yicI_8) BcellWH2_04293(yicI_9)
PDI: BDI_3102
DORI: FH5T_00770
RMR: Rmar_2605
CPI: Cpin_5548
PHE: Phep_2697
MGOT: MgSA37_01950(yicI_4) MgSA37_02212(yicI_5)
DFE: Dfer_1569
SLI: Slin_3567
LBY: Lbys_2946
PSEZ: HME7025_00135(yicI)
FJO: Fjoh_0778
FJG: BB050_01792(yicI_1)
TMA: TM0308
TMW: THMA_0315
TMQ: THMB_0315
TMX: THMC_0315
TPT: Tpet_0609
TRQ: TRQ2_0623
TNP: Tnap_0947
IAG: Igag_0310
SSO: SSO3022(xylS)
SSOA: SULA_0800
SSOL: SULB_0802
SSOF: SULC_0800
SID: M164_2342
SII: LD85_2631
SIH: SiH_2275
SIR: SiRe_2222
SIC: SiL_2184
CMA: Cmaq_1660
ASC: ASAC_0772
ACIA: SE86_05890
 » show all
Taxonomy
Reference
1  [PMID:10801892]
  Authors
Moracci M, Cobucci Ponzano B, Trincone A, Fusco S, De Rosa M, van Der Oost J, Sensen CW, Charlebois RL, Rossi M
  Title
Identification and molecular characterization of the first alpha -xylosidase from an archaeon.
  Journal
J Biol Chem 275:22082-9 (2000)
DOI:10.1074/jbc.M910392199
  Sequence
[sso:SSO3022]
Reference
2  [PMID:11402218]
  Authors
Sampedro J, Sieiro C, Revilla G, Gonzalez-Villa T, Zarra I
  Title
Cloning and expression pattern of a gene encoding an alpha-xylosidase active against xyloglucan oligosaccharides from Arabidopsis.
  Journal
Plant Physiol 126:910-20 (2001)
  Sequence
[ath:AT1G68560]
Reference
3  [PMID:11859845]
  Authors
Crombie HJ, Chengappa S, Jarman C, Sidebottom C, Reid JS
  Title
Molecular characterisation of a xyloglucan oligosaccharide-acting alpha-D-xylosidase from nasturtium (Tropaeolum majus L.) cotyledons that resembles plant 'apoplastic' alpha-D-glucosidases.
  Journal
Planta 214:406-13 (2002)
Reference
4  [PMID:15501829]
  Authors
Lovering AL, Lee SS, Kim YW, Withers SG, Strynadka NC
  Title
Mechanistic and structural analysis of a family 31 alpha-glycosidase and its glycosyl-enzyme intermediate.
  Journal
J Biol Chem 280:2105-15 (2005)
DOI:10.1074/jbc.M410468200
  Sequence
[eco:b3656]
Reference
5  [PMID:16267099]
  Authors
Iglesias N, Abelenda JA, Rodino M, Sampedro J, Revilla G, Zarra I
  Title
Apoplastic glycosidases active against xyloglucan oligosaccharides of Arabidopsis thaliana.
  Journal
Plant Cell Physiol 47:55-63 (2006)
DOI:10.1093/pcp/pci223
  Sequence
[ath:AT1G68560]
Reference
6  [PMID:16631751]
  Authors
Okuyama M, Kaneko A, Mori H, Chiba S, Kimura A
  Title
Structural elements to convert Escherichia coli alpha-xylosidase (YicI) into alpha-glucosidase.
  Journal
FEBS Lett 580:2707-11 (2006)
DOI:10.1016/j.febslet.2006.04.025
  Sequence
[eco:b3656]
Reference
7  [PMID:21426303]
  Authors
Larsbrink J, Izumi A, Ibatullin FM, Nakhai A, Gilbert HJ, Davies GJ, Brumer H
  Title
Structural and enzymatic characterization of a glycoside hydrolase family 31 alpha-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification.
  Journal
Biochem J 436:567-80 (2011)
DOI:10.1042/BJ20110299
Other DBs
ExplorEnz - The Enzyme Database: 3.2.1.177
IUBMB Enzyme Nomenclature: 3.2.1.177
ExPASy - ENZYME nomenclature database: 3.2.1.177
BRENDA, the Enzyme Database: 3.2.1.177

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