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Database: UniProt
Entry: A6VKN2_ACTSZ
LinkDB: A6VKN2_ACTSZ
Original site: A6VKN2_ACTSZ 
ID   A6VKN2_ACTSZ            Unreviewed;       796 AA.
AC   A6VKN2;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Alpha-glucosidase {ECO:0000313|EMBL:ABR73529.1};
DE            EC=3.2.1.20 {ECO:0000313|EMBL:ABR73529.1};
GN   OrderedLocusNames=Asuc_0149 {ECO:0000313|EMBL:ABR73529.1};
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR73529.1, ECO:0000313|Proteomes:UP000001114};
RN   [1] {ECO:0000313|Proteomes:UP000001114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC   {ECO:0000313|Proteomes:UP000001114};
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 31 family.
CC       {ECO:0000256|ARBA:ARBA00007806, ECO:0000256|RuleBase:RU361185}.
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DR   EMBL; CP000746; ABR73529.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VKN2; -.
DR   STRING; 339671.Asuc_0149; -.
DR   CAZy; GH31; Glycoside Hydrolase Family 31.
DR   KEGG; asu:Asuc_0149; -.
DR   eggNOG; COG1501; Bacteria.
DR   HOGENOM; CLU_000631_7_2_6; -.
DR   OrthoDB; 176168at2; -.
DR   Proteomes; UP000001114; Chromosome.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0032450; F:maltose alpha-glucosidase activity; IEA:UniProtKB-EC.
DR   CDD; cd06599; GH31_glycosidase_Aec37; 1.
DR   CDD; cd14752; GH31_N; 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; 2.
DR   InterPro; IPR033403; DUF5110.
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; PTHR22762; ALPHA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR22762:SF165; PUTATIVE (AFU_ORTHOLOGUE AFUA_1G06560)-RELATED; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:ABR73529.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU361185, ECO:0000313|EMBL:ABR73529.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001114}.
FT   DOMAIN          27..213
FT                   /note="Glycoside hydrolase family 31 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13802"
FT   DOMAIN          263..586
FT                   /note="Glycoside hydrolase family 31 TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01055"
FT   DOMAIN          596..683
FT                   /note="Glycosyl hydrolase family 31 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21365"
FT   DOMAIN          701..767
FT                   /note="DUF5110"
FT                   /evidence="ECO:0000259|Pfam:PF17137"
SQ   SEQUENCE   796 AA;  92434 MW;  07ED18D26C016F2F CRC64;
     MKTLKSAQFL RQEGNRVDIQ CERDYIMHIF VLEQDVIRVA FTHKNAFKLD RTWAIAPNQE
     DVPFEGRDRI STAGFSLPNY QLNFTNDVIE VATDLLKIRI NQPLALEWFY KKEDEWLPLM
     QERKTGAYQF GVSNDKIAHF IARSLDENCY GLGEKAGDLN RKGRRFEMRN LDAMGYNAEK
     TDPLYKHIPF YITRKNDVSY GIYYDNLAQC WFDLGNELDN YHTAYKSYRA EDGDMDYYVI
     LGPSTLDVTK KYTALTGGTI FGPRWGLGYS GSTMSYTDAD DAQEQLKKFV DLCKQHDIPC
     DSFQLSSGYT SINGKRYVFN WNYDKIPEPL KMSAHFREAG MHLAANIKPC MLQDHPRYKE
     AETLGLFIKD SETGLPERSV FWDDEGSHLD FTNPATVKWW KDNVKEQLLE RGIGSTWNDN
     NEYEIWDEQA KCAGFGKEIP INLIRALHPL LMMRSSYEAQ KEFAPNERPY LISRSGCAGM
     NRYVQTWSGD NRTGWNTLRY NIRMGLGMSL SGLYNVGHDV GGFAGDKPEP ELFVRWVQNG
     IFHPRFTIHS WNDDKTVNEP WMYPEVTNII RDTIKLRYRL MPYIYNIFWQ SHKQLEPMLR
     PTFLDHENDA NTYAETDDYL FGRELLVASV VEKGQRNREV YLPQNHAGWY DFYHHTYYEP
     GQKINVDAPL ERIPLFVKAG TVIPMSERTA YSKPEADTAR QLAVYPLKQD GELQCSIFDD
     DGLTYQYQKG EYLQLNITLG STQDTVYMDI RKQGNWKPAY QALKLTLPAN ETRTFLVNGN
     EFRPGTELSL ENIREI
//
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