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Database: UniProt
Entry: A0A4R7T845_9ACTN
LinkDB: A0A4R7T845_9ACTN
Original site: A0A4R7T845_9ACTN 
ID   A0A4R7T845_9ACTN        Unreviewed;      1076 AA.
AC   A0A4R7T845;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   28-JAN-2026, entry version 20.
DE   SubName: Full=Alpha-glucosidase (Family GH31 glycosyl hydrolase) {ECO:0000313|EMBL:TDU88074.1};
GN   ORFNames=EV138_1613 {ECO:0000313|EMBL:TDU88074.1};
OS   Kribbella voronezhensis.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Kribbellaceae; Kribbella.
OX   NCBI_TaxID=2512212 {ECO:0000313|EMBL:TDU88074.1, ECO:0000313|Proteomes:UP000295151};
RN   [1] {ECO:0000313|EMBL:TDU88074.1, ECO:0000313|Proteomes:UP000295151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2575 {ECO:0000313|EMBL:TDU88074.1,
RC   ECO:0000313|Proteomes:UP000295151};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAR-2019) 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:TDU88074.1}.
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DR   EMBL; SOCE01000001; TDU88074.1; -; Genomic_DNA.
DR   RefSeq; WP_133977758.1; NZ_SOCE01000001.1.
DR   AlphaFoldDB; A0A4R7T845; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000295151; 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; 1.
DR   CDD; cd06595; GH31_u1; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR   InterPro; IPR005084; CBM6.
DR   InterPro; IPR033403; DUF5110.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR017853; GH.
DR   InterPro; IPR048395; Glyco_hydro_31_C.
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; PF03422; CBM_6; 2.
DR   Pfam; PF17137; DUF5110; 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; SSF49785; Galactose-binding domain-like; 2.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   PROSITE; PS51175; CBM6; 2.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:TDU88074.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000295151};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1076
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038777859"
FT   DOMAIN          150..279
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   DOMAIN          300..429
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
SQ   SEQUENCE   1076 AA;  113580 MW;  D75D8A9509257543 CRC64;
     MRTRTATTFR RLCALALAAC AIAASTVALP ASSATATADS RTIVAGNARF QVLSPTLIRT
     EYAGDGQFQD ASTFNAVGRN AFPATPFTSS ISGGVLTIRT RATTLTYRLG SGPFDAGNLS
     LNLNAGTAGT AGTAAVAAAP WHRLTCPVGA LCEAEDLTAD GLGTATDHNG YTGGGFLAGF
     ETTGAQASAD VSATTAGTYT LTTRYANGTG GDGKHEVRTL SLSVDGGAPT TLTFAPTDGW
     DSWALASAPI TLGAGHHVVR LSRSAADSGN VNVDSFAILK AGSGYPPASA RAYGDCAFGV
     SCEAEAGLPG GSAKLASDHP AYAGRGFIDE LNDGSSLTQR IVGVPADGTY QLSLRYANGT
     GGDGKHETRT AAVTAAGVTR TASFPATTDW DTWSTTSVPV DLKAGTNEVV LGCPGTTSCH
     VNLDTLAVTT IGVPAPQPHL ALGGYRRGLD GVNGDNGTPS TTEGLLHRDG WYLLDDTTSA
     LYDTGSRRTT QRPAHGASPY QDGYVFAFGH DYKAGLGDLA TLTGPPQLLP RWAYGVWYSE
     YFDRTAADYR DTILPRFRAN GVPLDVLVTD TDFKAPDTWN GWQFDRTKFP DPAGFFAWSK
     SQGLHNNLNV HPSIMGSDPQ FAQAQATAKG KLTKSGCGTD CYVFDWSDPD QLKAYLDLHR
     EMMRQGNDFW WLDWCCDSSR SSLPGVTPDA WINQQYADLA APAIGRGFVI SRAYGSLQAG
     GYGGPIGLAT GPWADKRSTL HFTGDTSSTW GTLAMEVGVT PAESAATGMS AISHDIGGHN
     DTTGLPGSEI YTSGGQQRRT AKLPDDMYAR WVQLGTFQPI DRLHSNHSDR LPWQYGTAAA
     QSATRFLNLR ENLVPYTYTL AQQAATTGVP VVRPTYLEYP EEPTAYTAAG SEYFYGPDLL
     VAPVTTPGTQ ATTTVWFPPG QWTDYFTGKT YAGGTTQQIT TGLDTMPVFL RAGGIMTTRT
     ANVANDGQNP LTKATATVAT GANGTFTLYE DNGSTTNKSQ STRTGLTYTE NHGRHTLTIG
     PSQGRFPGQV SAREWTVKFL GVPTAPAKVS GSRNWSWDAT TRSLTVQVSS THRISF
//
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