ID C6WNT1_ACTMD Unreviewed; 693 AA.
AC C6WNT1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Alpha-galactosidase {ECO:0000256|RuleBase:RU361168};
DE EC=3.2.1.22 {ECO:0000256|RuleBase:RU361168};
DE AltName: Full=Melibiase {ECO:0000256|RuleBase:RU361168};
GN OrderedLocusNames=Amir_1044 {ECO:0000313|EMBL:ACU35000.1};
OS Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064
OS / NCIMB 13271 / NRRL B-12336 / IMRU 3971 / 101).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinosynnema.
OX NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU35000.1, ECO:0000313|Proteomes:UP000002213};
RN [1] {ECO:0000313|EMBL:ACU35000.1, ECO:0000313|Proteomes:UP000002213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29888 / DSM 43827 / JCM 3225 / NBRC 14064 / NCIMB 13271 /
RC NRRL B-12336 / IMRU 3971 / 101 {ECO:0000313|Proteomes:UP000002213};
RX PubMed=21304636; DOI=10.4056/sigs.21137;
RA Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D., Goodwin L.,
RA Pitluck S., Rohde M., Goker M., Pati A., Ivanova N., Mavromatis K.,
RA Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Han C., Chain P., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL Stand. Genomic Sci. 1:46-53(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing alpha-D-galactose
CC residues in alpha-D-galactosides, including galactose
CC oligosaccharides, galactomannans and galactolipids.; EC=3.2.1.22;
CC Evidence={ECO:0000256|RuleBase:RU361168};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 27 family.
CC {ECO:0000256|ARBA:ARBA00009743, ECO:0000256|RuleBase:RU361168}.
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DR EMBL; CP001630; ACU35000.1; -; Genomic_DNA.
DR AlphaFoldDB; C6WNT1; -.
DR STRING; 446462.Amir_1044; -.
DR CAZy; CBM51; Carbohydrate-Binding Module Family 51.
DR CAZy; GH27; Glycoside Hydrolase Family 27.
DR KEGG; ami:Amir_1044; -.
DR eggNOG; COG3345; Bacteria.
DR HOGENOM; CLU_013093_3_2_11; -.
DR Proteomes; UP000002213; Chromosome.
DR GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd14792; GH27; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.120.1060; NPCBM/NEW2 domain; 1.
DR InterPro; IPR018905; A-galactase_NEW3.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013222; Glyco_hyd_98_carb-bd.
DR InterPro; IPR002241; Glyco_hydro_27.
DR InterPro; IPR000111; Glyco_hydro_27/36_CS.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR041233; Melibiase_C.
DR InterPro; IPR038637; NPCBM_sf.
DR PANTHER; PTHR11452:SF75; ALPHA-GALACTOSIDASE; 1.
DR PANTHER; PTHR11452; ALPHA-GALACTOSIDASE/ALPHA-N-ACETYLGALACTOSAMINIDASE; 1.
DR Pfam; PF16499; Melibiase_2; 1.
DR Pfam; PF17801; Melibiase_C; 1.
DR Pfam; PF08305; NPCBM; 1.
DR Pfam; PF10633; NPCBM_assoc; 1.
DR PRINTS; PR00740; GLHYDRLASE27.
DR SMART; SM00776; NPCBM; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR PROSITE; PS00512; ALPHA_GALACTOSIDASE; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|RuleBase:RU361168};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361168};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361168};
KW Reference proteome {ECO:0000313|Proteomes:UP000002213};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 547..692
FT /note="Glycosyl hydrolase family 98 putative carbohydrate-
FT binding module"
FT /evidence="ECO:0000259|SMART:SM00776"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 693 AA; 73808 MW; 3500969C8FDE82C0 CRC64;
MDESTNAAGD APVDQDGTTG DGAVSGGTAG GSSADDSAAG SGAAGSGAAE TGAPQEIRPP
ALAPTPPMGF NNWNSTQCGP EFTDSMIRGI ADLFLSLGLK DAGYEYVNID DCWALPQRDA
DGDLVPDPVR FPEGMKPLVD YVHSKGLKFG IYTSAGTRTC SERGFPGALG HERQDAALFA
SWGVDYLKYD NCHNQGVDAR LRYRAMRDAI AATGRPIVLS VCEWGENRPW EWAFEVGQLW
RTTPDIRDSW DSVLEIAKAN MALAEHAGPN RWNDPDMLEV GNGGLTWEEC RTHFSLWAMM
AAPLLIGVDL RSVAPEAVEI LTNREVIALD QDPLGEQARV VRSEDGLHVL VKRLQDGGRA
VALFNENDVP ARISTSAAEA GLPRSTGYRL RDVWARTDAH SAGDVTAWVP PHGAVVYRVT
PEPAWLLLPP AVDAGVEPVL SRPGALPLVD PDAPSLVTTS LGDNGWLPVL GARVDLEAPA
GWRVRPRGQR ARSVLAGGDR LDTTWEVLPP AGLEPGRYRL TALFAYLYGW GRRVSADLEV
VVPHRLPSGT SYLSDAPWLR ASNGFGPVEV DTSNGEAEAG DGGPLTVNGR VFEKGLGVHA
PSSVEYFTGG RCTSVSAFVG VDDEKPAAGS VVFQVWADER KVADSGALTT RDDAVELVAD
VTGARTVRLV VTDAGNGVDS DHGDWCDLKA TCE
//