GenomeNet

Database: UniProt
Entry: A0A1M6FGQ1_9RHOB
LinkDB: A0A1M6FGQ1_9RHOB
Original site: A0A1M6FGQ1_9RHOB 
ID   A0A1M6FGQ1_9RHOB        Unreviewed;       453 AA.
AC   A0A1M6FGQ1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Alpha-galactosidase {ECO:0000313|EMBL:SHI96823.1};
GN   ORFNames=SAMN05444417_2305 {ECO:0000313|EMBL:SHI96823.1};
OS   Wenxinia saemankumensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Wenxinia.
OX   NCBI_TaxID=1447782 {ECO:0000313|EMBL:SHI96823.1, ECO:0000313|Proteomes:UP000184292};
RN   [1] {ECO:0000313|EMBL:SHI96823.1, ECO:0000313|Proteomes:UP000184292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100565 {ECO:0000313|EMBL:SHI96823.1,
RC   ECO:0000313|Proteomes:UP000184292};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
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; FQYO01000004; SHI96823.1; -; Genomic_DNA.
DR   RefSeq; WP_073330428.1; NZ_FQYO01000004.1.
DR   AlphaFoldDB; A0A1M6FGQ1; -.
DR   STRING; 1447782.SAMN05444417_2305; -.
DR   OrthoDB; 9767022at2; -.
DR   Proteomes; UP000184292; 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; IPR019802; GlycHydrolase_4_CS.
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.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184292}.
FT   DOMAIN          195..417
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         148
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         170
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         200
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            110
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   453 AA;  50978 MW;  CE92344F905245C5 CRC64;
     MTIVTFIGAG STVFAKNLAG DILQREALKG ATIRLMDIDP GRLEESEIVV SKMAKTLGGH
     ATVETYTDRR RALTGADFVI CCFQVGGYEP CTVTDFEVPK KFGLRQTIAD TLGIGGIMRG
     LRTVPVLWDI CEDMLAVCPH AIMLQYVNPM AINTWAIGAK YPQIRQVGLC HSVQGTAEEL
     ARDLGIPIGE IRYHCAGINH MAYYTRFEQR LPDGTYKDLY PELKRGYAEG RLPRFSNHSD
     RCPNKVRYEM MMRLGYFVTE SSEHFAEYVP YFIKKDRPDL IERFGIPLDE YPKRCVEQVE
     RWQAQAQKYR EAETVEVKPS HEYASEIINS VVTGSPSVIY GNIPNRGYIP QLPEGAAVEV
     PVLVDGNGLQ PTVRTGIPPQ LIALMRTNVN VQELTVAALM EENPEHIYHA AMLDPHTGSE
     LDLDQIWELT HELLAAHGEW LPEWARPERR KSA
//
DBGET integrated database retrieval system