ID E4Q987_CALH1 Unreviewed; 903 AA.
AC E4Q987;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Mannan endo-1,4-beta-mannosidase {ECO:0000313|EMBL:ADQ08136.1};
DE EC=3.2.1.78 {ECO:0000313|EMBL:ADQ08136.1};
GN OrderedLocusNames=Calhy_2438 {ECO:0000313|EMBL:ADQ08136.1};
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:ADQ08136.1, 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:ADQ08136.1, 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 26 family.
CC {ECO:0000256|ARBA:ARBA00007754, ECO:0000256|PROSITE-ProRule:PRU01100}.
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; CP002219; ADQ08136.1; -; Genomic_DNA.
DR RefSeq; WP_013404277.1; NC_014652.1.
DR AlphaFoldDB; E4Q987; -.
DR STRING; 632292.Calhy_2438; -.
DR CAZy; CBM27; Carbohydrate-Binding Module Family 27.
DR CAZy; CBM35; Carbohydrate-Binding Module Family 35.
DR CAZy; GH26; Glycoside Hydrolase Family 26.
DR KEGG; chd:Calhy_2438; -.
DR eggNOG; COG4124; Bacteria.
DR HOGENOM; CLU_320992_0_0_9; -.
DR OrthoDB; 9802773at2; -.
DR Proteomes; UP000006890; Chromosome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016985; F:mannan endo-1,4-beta-mannosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006080; P:substituted mannan metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR015295; Carb-bd_module_27.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR000805; Glyco_hydro_26.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR40079:SF4; GH26 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR40079; MANNAN ENDO-1,4-BETA-MANNOSIDASE E-RELATED; 1.
DR Pfam; PF09212; CBM27; 2.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF02156; Glyco_hydro_26; 1.
DR PRINTS; PR00739; GLHYDRLASE26.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS51764; GH26; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PROSITE-
KW ProRule:PRU01100};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01100}.
FT DOMAIN 442..566
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 589..892
FT /note="GH26"
FT /evidence="ECO:0000259|PROSITE:PS51764"
FT ACT_SITE 743
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
FT ACT_SITE 835
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01100"
SQ SEQUENCE 903 AA; 102065 MW; 58DF710C27D61CD5 CRC64;
MRKGLKIASL IVSLVFLLGL LPTGIFGAVE TSVQSYVFDF EDGTTMTFDE AWGDSLKCIK
KVSVSTDLQR PGNKYALRLD VEFNENNGWD QGDLGAWIGG VVEGQFDFTN YKSVEFEMFV
PYDEFAKAKG GFAYKVVLND GWKELGSEFS ITVNAGKKVK INGKDYMVIH KAFAIPDDFR
TKKRAQLVFQ FAGQNCNYKG PIYLDNIRIR PEDASNLSKE DYGSSEEEEI VENFFTGVTL
VYPVEGKNFV YNFEKDTMGF YKYSGDGFAK KTKSMEFSQD LKTSTNAGSL KLNANFQGTA
FEEMNIAVKL TDKEGKLFDL GKYSTLEYTI YIPNPDKVAG KIMSASAVDS PWKIIKDFTA
LNYKDKTTWK EINGKTYAVI KCKDNLYNVR EKAGVLVLRI AGSYVKYTGP IYIDNVALIA
GKKVAPKVER ISLPNPKTYY KVKIEAESAS DGWAYSVEKE NAKFSGKGYV LLFGNNMGNT
LYNIKVPKTG HYIFTLAIST LGLVKDGSID IWIDGDLKGG AKVPNVKGKF QEVVVRKKIY
LTEGEHTISL QKSGGYTIAV DYFVIEELVA ANKSKLSVSS KLVTPNPHPN AQRLMNYLAS
IYGEKILSGQ QSSGEGKEVQ MIFDVTRRYP AVRSFDLMDY SPSRMQRGTK GTDVDEAIKW
WKNGGIVAFC WHWNAPTGLI DQPGKEWWRG FYTEATTFDL KKAMDNPNSE EYKLILRDID
AIAQQFKKLQ AEGVPVLFRP LHEASGGWFW WGAKGAEPYI KLWKLMFDRL VNYHKVNNLI
WVWNGQDAAW YPGDQYVDII AEDIYEEKAQ YSPYTERFVK ALKYTNSNKM IALSECGTIP
DPAVLKQEGV SWLWFSVWAG GYVMTGSKYN DEWNDNHMLR KIYNSDYVIT KDELPDIKSI
PLE
//
