ID E4QDM3_CALH1 Unreviewed; 670 AA.
AC E4QDM3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Glycoside hydrolase family 31 {ECO:0000313|EMBL:ADQ06440.1};
GN OrderedLocusNames=Calhy_0703 {ECO:0000313|EMBL:ADQ06440.1};
OS Caldicellulosiruptor hydrothermalis (strain DSM 18901 / VKM B-2411 / 108).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=632292 {ECO:0000313|EMBL:ADQ06440.1, ECO:0000313|Proteomes:UP000006890};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=108;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., Blumer-Schuette S.E., Kelly R.M., Woyke T.;
RT "Complete sequence of Caldicellulosiruptor hydrothermalis 108.";
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ06440.1, ECO:0000313|Proteomes:UP000006890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18901 / VKM B-2411 / 108
RC {ECO:0000313|Proteomes:UP000006890};
RX PubMed=21216991; DOI=10.1128/JB.01515-10;
RA Blumer-Schuette S.E., Ozdemir I., Mistry D., Lucas S., Lapidus A.,
RA Cheng J.F., Goodwin L.A., Pitluck S., Land M.L., Hauser L.J., Woyke T.,
RA Mikhailova N., Pati A., Kyrpides N.C., Ivanova N., Detter J.C.,
RA Walston-Davenport K., Han S., Adams M.W., Kelly R.M.;
RT "Complete genome sequences for the anaerobic, extremely thermophilic plant
RT biomass-degrading bacteria Caldicellulosiruptor hydrothermalis,
RT Caldicellulosiruptor kristjanssonii, Caldicellulosiruptor kronotskyensis,
RT Caldicellulosiruptor owensenis, and Caldicellulosiruptor lactoaceticus.";
RL J. Bacteriol. 193:1483-1484(2011).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR EMBL; CP002219; ADQ06440.1; -; Genomic_DNA.
DR RefSeq; WP_013402640.1; NC_014652.1.
DR AlphaFoldDB; E4QDM3; -.
DR STRING; 632292.Calhy_0703; -.
DR CAZy; GH31; Glycoside Hydrolase Family 31.
DR KEGG; chd:Calhy_0703; -.
DR eggNOG; COG1501; Bacteria.
DR HOGENOM; CLU_000631_7_3_9; -.
DR OrthoDB; 176168at2; -.
DR Proteomes; UP000006890; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd06591; GH31_xylosidase_XylS; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE, INTESTINAL-LIKE; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|RuleBase:RU361185};
KW Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:ADQ06440.1}.
FT DOMAIN 24..183
FT /note="Glycoside hydrolase family 31 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13802"
FT DOMAIN 231..566
FT /note="Glycoside hydrolase family 31 TIM barrel"
FT /evidence="ECO:0000259|Pfam:PF01055"
FT DOMAIN 576..660
FT /note="Glycosyl hydrolase family 31 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21365"
SQ SEQUENCE 670 AA; 77744 MW; 75BFF018B436FD19 CRC64;
MSILTFTDNK LIRKFDGETI WIEPWGKNAL RIRCTRLAKM PEENWALLPV NSSEVEVKVN
GNSGFIRNGN VIAEINEYGF IKIKNSKGDV LLEEYWQTRI DKNNKISLQI PGRELKPIPG
GLYKAKVVFK GCNDEKMYGL GQHQEPFLNL KGCEFELSQR NSQATVPFII SNRGYGFLWN
NPAVGRVTFA KNGTQWVAEV TKTIDYWVTT GENIEEIIEN YTEVTGRYPP IPYFATGFWQ
SKLRYHSQDE VLEVAREYKK RGLPLSVIVI DFFHWPQQGE WRFDPKYWPD PEKMVKELKD
MGIEVMVSIW PTVDPRSCNY QEMKEKGYLV QTDRGIRTQM LCQGNEVFVD FTNPEAGEYV
WNKVKENYFK YGIRIFWLDE AEPEYSVYDF DNYRYSLGPC LEVGNIYPFY YAKAFYEGLK
KEGINDVLNL VRCAWAGSQR YGALVWSGDI HSNFKTLRKQ VAAGLNMALS GIALWTTDIG
GFFGGDPKDP KFQELIVRWF QYGVFCPVCR LHGYREPTAQ DVGNNDTGMH DFDTCGPNEV
WSFGDKAYEI IKELLFLRER LRPYIAEQFK LTHERGTPIM RPLFYDFPQD DITWEIEDEY
MFGPDILVAP VLYEGATSRR VYLPAGVKWV DVNYGKIYEG GQWIDSYYAP LEVVPVFVRE
SAPVLDCFRR
//
