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Database: UniProt
Entry: I0IAS1_PHYMF
LinkDB: I0IAS1_PHYMF
Original site: I0IAS1_PHYMF 
ID   I0IAS1_PHYMF            Unreviewed;       480 AA.
AC   I0IAS1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Putative alpha-galactosidase {ECO:0000313|EMBL:BAM02359.1};
DE            EC=3.2.1.22 {ECO:0000313|EMBL:BAM02359.1};
GN   OrderedLocusNames=PSMK_02000 {ECO:0000313|EMBL:BAM02359.1};
OS   Phycisphaera mikurensis (strain NBRC 102666 / KCTC 22515 / FYK2301M01).
OC   Bacteria; Planctomycetota; Phycisphaerae; Phycisphaerales;
OC   Phycisphaeraceae; Phycisphaera.
OX   NCBI_TaxID=1142394 {ECO:0000313|EMBL:BAM02359.1, ECO:0000313|Proteomes:UP000007881};
RN   [1] {ECO:0000313|EMBL:BAM02359.1, ECO:0000313|Proteomes:UP000007881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102666 / KCTC 22515 / FYK2301M01
RC   {ECO:0000313|Proteomes:UP000007881};
RA   Ankai A., Hosoyama A., Terui Y., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Yamada-Narita S., Kawakoshi A., Fukunaga Y., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Phycisphaera mikurensis NBRC 102666.";
RL   Submitted (FEB-2012) 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}.
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DR   EMBL; AP012338; BAM02359.1; -; Genomic_DNA.
DR   AlphaFoldDB; I0IAS1; -.
DR   STRING; 1142394.PSMK_02000; -.
DR   KEGG; phm:PSMK_02000; -.
DR   PATRIC; fig|1142394.8.peg.203; -.
DR   eggNOG; COG1486; Bacteria.
DR   HOGENOM; CLU_045951_1_1_0; -.
DR   Proteomes; UP000007881; Chromosome.
DR   GO; GO:0004557; F:alpha-galactosidase activity; IEA:UniProtKB-EC.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007881}.
FT   DOMAIN          198..452
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   BINDING         151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         203
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   SITE            113
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   480 AA;  52614 MW;  6F5C265A74FA4C38 CRC64;
     MPRPVHLTFL GAGSNFCSTL CRDLLLIPGN AGGELRLVDV DRGRLDRMHR VIEKLIEATG
     NADKWKVVSS TDRRAVLPGT HYAVCCVEVS GVDCVAWDND IPLKHGIDQC IGDTLGPGGL
     FKALRTVPVF LDALRDMREL CPGALMLNYT NPMGILCLAA GRAVPEVPVV GLCHSVQGTS
     HLLAEYAGVD YETLRWECAG INHLAWFTKL ERNGEDLYAK TLRAKFEAEV AAGFAEAEAG
     VAVHDAQDAV FGEEKEQPYE GRDLVRKDMC LQFGAFITES SGHLSEYLPW YRKNERGRAL
     LRRGYDGGSR FYATNWPHWR TEADALRDRL VSGEEQIDLK RSWEYGTFII EAIEKDAPWR
     IHGNVMNRVA DPAKASPGEA GKLITNLPGD GCVEVACLVD GNGVQPTRYG ALPAPMARVC
     ASNMAFIDLA ATAVIQRSKE AAVHALLLDP LTAAVLSPAQ IREMAMEMFE AEKDFLPGYA
//
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