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Database: UniProt
Entry: A0A140LC27_9FIRM
LinkDB: A0A140LC27_9FIRM
Original site: A0A140LC27_9FIRM 
ID   A0A140LC27_9FIRM        Unreviewed;       726 AA.
AC   A0A140LC27;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   SubName: Full=Oligosaccharide 4-alpha-D-glucosyltransferase {ECO:0000313|EMBL:KXG78102.1};
DE            EC=2.4.1.161 {ECO:0000313|EMBL:KXG78102.1};
GN   ORFNames=AN619_02900 {ECO:0000313|EMBL:KXG78102.1};
OS   Thermotalea metallivorans.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales;
OC   Thermotaleaceae; Thermotalea.
OX   NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG78102.1, ECO:0000313|Proteomes:UP000070456};
RN   [1] {ECO:0000313|EMBL:KXG78102.1, ECO:0000313|Proteomes:UP000070456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2-1 {ECO:0000313|EMBL:KXG78102.1,
RC   ECO:0000313|Proteomes:UP000070456};
RA   Patel B.K.;
RT   "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT   isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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:KXG78102.1}.
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DR   EMBL; LOEE01000007; KXG78102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A140LC27; -.
DR   STRING; 520762.AN619_02900; -.
DR   PATRIC; fig|520762.4.peg.325; -.
DR   Proteomes; UP000070456; 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:0033825; F:oligosaccharide 4-alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06604; GH31_glucosidase_II_MalA; 1.
DR   CDD; cd14752; GH31_N; 1.
DR   Gene3D; 2.60.40.4040; -; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR017853; GH.
DR   InterPro; IPR030458; Glyco_hydro_31_AS.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
DR   InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR   InterPro; IPR000322; Glyco_hydro_31_TIM.
DR   PANTHER; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF120; HETEROGLYCAN GLUCOSIDASE 1; 1.
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; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361185};
KW   Glycosyltransferase {ECO:0000313|EMBL:KXG78102.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361185};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070456};
KW   Transferase {ECO:0000313|EMBL:KXG78102.1}.
FT   DOMAIN          47..128
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          172..531
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          543..629
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          647..699
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
SQ   SEQUENCE   726 AA;  84887 MW;  FA2898CFFB6FD8F3 CRC64;
     MGLQVITMKV YRIHEKITKY RFGNPFPTDG VLVKGDPWEK EGMDYFQVEQ GTEIRLTYKM
     DSKDMVWGLG ENQRGMNKRG GIYVSYCSDD PRHTPDKKSL YGAHNFMIVD GRERFGLFID
     YPGQVAFDVG FSHTDVIEII IDGTDADIYI IDGEGLREIV RKFFHIIGEG YAPPKWAFGY
     QQSRWSYPDA KTIEGVAEAF IDHDIPCDAI YLDIDYMEGF KDFTVSEDRF PDFPRFVEKM
     REKGFRLVPI IDAGVKIEKG YGVYEEGIQG GYFCTDGEGK PFVAAVWPGK VHFPDFLNPE
     ARRWFGLKYK GLIDWGIEGF WNDMNEPAIF YTERGLKKGI ELAKQSENEN LDMDSFFALK
     DAFIHMSNHR EDYQSMYHHV DGKQVNHHEV HNLYGYYMTR AAAEGFEEIA PNKRFLLFSR
     ASYIGMHRFG GIWTGDNHSW WEHILLNLKM MPSLNMCGFL YAGADTGGFG GDANAQLLIR
     WTQFSLFTPL FRNHSAIGGR RQEPFSFDQE TTEMIRKAIQ FRYALIPYIY SEYMKALLHR
     DMYMLPLAFA YEDEISRRVE NQLLVGDGLM IAPIYEENAL GRYVWLPEDM LLWKVDDYRE
     RSYEIKRKGH LYLEVGLHEI PVFIRKNKML IFGNHGRNTE VLDHRELYVV AFIEDRAQYV
     YYDDDGLTKD YKKEKYTEIR ISIERREEDF EIKIENRENR QVKRIHFEMV DIHGNIAKKT
     VVLAAQ
//
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