ID   A0A2K2F7Z8_9CLOT        Unreviewed;      1284 AA.
AC   A0A2K2F7Z8;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   SubName: Full=Glycosyl hydrolase family 31 {ECO:0000313|EMBL:PNT95506.1};
GN   ORFNames=CDQ84_16970 {ECO:0000313|EMBL:PNT95506.1};
OS   Clostridium thermosuccinogenes.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=84032 {ECO:0000313|EMBL:PNT95506.1, ECO:0000313|Proteomes:UP000236151};
RN   [1] {ECO:0000313|EMBL:PNT95506.1, ECO:0000313|Proteomes:UP000236151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5806 {ECO:0000313|EMBL:PNT95506.1,
RC   ECO:0000313|Proteomes:UP000236151};
RA   Koendjbiharie J.G., van Kranenburg R.;
RT   "Investigating the central metabolism of Clostridium thermosuccinogenes.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PNT95506.1}.
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DR   EMBL; NIOJ01000065; PNT95506.1; -; Genomic_DNA.
DR   RefSeq; WP_103082932.1; NZ_CP021850.1.
DR   KEGG; cthd:CDO33_10355; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000236151; Unassembled WGS sequence.
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; cd04083; CBM35_Lmo2446-like; 2.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
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; 2.
DR   InterPro; IPR005084; CBM6.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR017853; GH.
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; IPR051816; Glycosyl_Hydrolase_31.
DR   PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR   PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE; 1.
DR   Pfam; PF16990; CBM_35; 2.
DR   Pfam; PF17137; DUF5110; 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; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51175; CBM6; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:PNT95506.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236151};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          859..991
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          997..1123
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
SQ   SEQUENCE   1284 AA;  143252 MW;  9177506A7E2A3E62 CRC64;
     MSIYDKNKSS INARFISLLI IFSIICSVTI LQSPITANAY ADTLGNVISA TANGDNVTII
     VDNGMEPGDD ILELQVCESD ILRVNYRPNG IASSPSTPII DPTRVWGSVG ASIDVNSDPI
     TISTSDMRIE IKRNPCRMTV KKPDGTVLFW EPDNAGVFHD GVRFQRPAGQ NMYGLHGYAC
     FDENGELLRN NTTAPAKAGQ QGNSGGPFMW STAGYGLLID SDGGYPVLES STNKMEFYYG
     DMIEEGRRYY KENVEYYIMF GDPENIMENY SRITGQAPMM PKWSMGFSNY EWGINQTELY
     NIVDTYRAKD IPIDSYGIDY DWKRYGEDNY GEFAWNTANF PDASSNLLKD TMLSKGIRLI
     GITKPRIVTK LQNGAWTKQG LDAQAGDYFY PGHAEYTDYF YPVTVRSIDP YKPAARDWFW
     QHSIDAFNKG IAGWWNDETD TVASGWANFW FGNFTTLHLS QAIYEGQRSY TNGQTRVWQT
     ARNYYPGTQR YATTIWSGDV GTQFHMNEHI WWTAGLNEQK ATMLSTINNG QMKWGSDGGG
     FNQNTGTTEN PSPELYTRWL QLAAFTPVFR VHGTFQHQRQ PWYYGFTAEE SSKAAIRLRY
     ALLPYVYSYE YKAYEKGVGL VKPLLYDYPN DPNVANYSDA WMFGDWLLVA PVTERYQTTK
     WIYLPAGEWI DYFTGIVYNG GQYIPYAVNG ESWTDIPLFI KKGAIIPSQE VLNYADEKAV
     TDIFVDIFPD MAASTFNFYD DDGQTYNYEN GQYFKQVFTA QDLGGSGINV SVSAKSGSYA
     SPIKYYYLKI HGKAAQTVSI NGVSSVPSYP NIYALRSGVG EGYAVGKDIY GDVTYVKIAA
     GAQKNVTING SVAQSADRMT YEAEEASLWG KTVATKAGYN TNHTGYTGLG FADRFENDGA
     AVTFDAKVKV GGEFPVDIRY ANGSSENRTM SVYVNGTFIR QVSFAPTGNW DTWGTSTQML
     PLVAGRNSIT IKYEASMGDT GFLNIDNISV PFYPETAVFE AESAALYGTA ARKTDHWFYS
     GSGFVAGMES VGAEVAFKVD VPQSGSYDTM LRYCNANGVA KTLNVYVNGV YQTTANLASS
     GYDWNVWSDW ANTFNLQKGQ NTISFRFDSG NSGYVNLDSL QVNLAAPTAH VERNILDNGG
     FERPTWDSSK WTEWHPAGQA LAYGVDSGIG TNPPEAAREG EQRAYFYHGS AYSQSIHQTA
     NIENGVYKLE FWARQFNTAP YTARAEVMEY GGNTIYFDIP QSTEWRHYVI DNISVTTGYI
     DIGFYVNSPG GTTLHLDGVR LIKK
//