ID A0A0S8IW09_9BACT Unreviewed; 443 AA.
AC A0A0S8IW09;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Alpha-mannosidase {ECO:0000313|EMBL:KPL01617.1};
GN ORFNames=AMK75_04240 {ECO:0000313|EMBL:KPL01617.1};
OS Planctomycetes bacterium SM23_65.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=1704030 {ECO:0000313|EMBL:KPL01617.1, ECO:0000313|Proteomes:UP000052185};
RN [1] {ECO:0000313|EMBL:KPL01617.1, ECO:0000313|Proteomes:UP000052185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_65 {ECO:0000313|EMBL:KPL01617.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|RuleBase:RU361152};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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:KPL01617.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJUT01000084; KPL01617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8IW09; -.
DR PATRIC; fig|1704030.3.peg.783; -.
DR Proteomes; UP000052185; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR Gene3D; 3.90.1820.10; AglA-like glucosidase; 1.
DR InterPro; IPR001088; Glyco_hydro_4.
DR InterPro; IPR022616; Glyco_hydro_4_C.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF6; ALPHA-GALACTOSIDASE; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW NAD {ECO:0000256|RuleBase:RU361152};
KW Nickel {ECO:0000256|PIRSR:PIRSR601088-3}.
FT DOMAIN 193..411
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 198
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 109
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 443 AA; 50083 MW; B69B8A07D61F9D44 CRC64;
MAKIAFIGAG SFGFTRGLVR DILTFPLLED ATLALMDINK ERLGFSTQAV KSIIADGNYP
AKVVSTTSRK RALEGADAAI VTILAGSTDV WKHDILIPKR FGIDTNVGDT RGPSGIFRAL
RTIPVMLDIC RDVERYAPDA ILLNYTNPMA MLCKAMLSQT KVKATGLCHS VQGTAAGLAR
MIGAPMDEIT YVCAGINHLS WFIRYEWNHK DAYPLIRKAL KKRRNYVREK VRNEMFRAFG
YYVTESSGHN SEYNWWFRKR PELIRKYCKP MKGSGWNAGE YAYILREYQS RRRTWRKRIR
RWIADHKDFS LARGHEYASN IINARMGGEM YKFNGNVLNE GIVTNLPQGC CVEVPVMATK
RGFEPIHVGA LPPQCAALTG LNAQIEDMAV EASATGNPEL VYQAICYDPL TAAVLSLAEI
RQMVKAMFRQ HRRYLPQFKT IRF
//