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Database: UniProt
Entry: A0A136KN59_9CHLR
LinkDB: A0A136KN59_9CHLR
Original site: A0A136KN59_9CHLR 
ID   A0A136KN59_9CHLR        Unreviewed;       461 AA.
AC   A0A136KN59;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Putative alpha-galactosidase {ECO:0000313|EMBL:KXK10884.1};
DE            EC=3.2.1.22 {ECO:0000313|EMBL:KXK10884.1};
GN   ORFNames=UZ14_CFX002003091 {ECO:0000313|EMBL:KXK10884.1};
OS   Chloroflexi bacterium OLB14.
OC   Bacteria; Chloroflexota; Tepidiformia.
OX   NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK10884.1, ECO:0000313|Proteomes:UP000070321};
RN   [1] {ECO:0000313|EMBL:KXK10884.1, ECO:0000313|Proteomes:UP000070321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB14 {ECO:0000313|EMBL:KXK10884.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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   -!- 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:KXK10884.1}.
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DR   EMBL; LMZR01000071; KXK10884.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136KN59; -.
DR   STRING; 1617415.UZ14_CFX002003091; -.
DR   Proteomes; UP000070321; Unassembled WGS sequence.
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}.
FT   DOMAIN          224..434
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         169
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         228
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   461 AA;  51462 MW;  C4C8C38E90BE6F96 CRC64;
     MTIITVIGAG SASFGENTLS ALLRSKKLKG STLRLVDRNA SSLDIVHRLA TRLNTEWEAG
     FNITAHTHHK DALQDSNFVV SAIEVGPREA LWKSDFEIPI KYGVRQPYAE NGGPGGFAHA
     ARNVKPVLEI VHDMELACPN AWFINFTNPM VRICDVVNRY SKIKVAGLCH QIYQGYMMAG
     VALAKDLNLQ VPDGLANTHA NILQHPLQQM MIHQAVPLLD IRAAGTNHFT WILSIHHKQT
     GEDLYPLLRK RFFELDESFE PLTRRIFHDF GLFPVPGDSH LCEYLPWMSD PITKPYESFN
     IQLYDWEVMA SVRDFSLDRL NEMANGNATI DGLLETDSEG ALELIENISQ AGSHYHLAVN
     LPNVGQIANL PKNAIVETPV HVGGAGVQPV HVGNLPEPIA ELCRREIMVA QLGIDAVVEG
     DYQKALQCLL LDPVITDMNV AKNILDDYLK TYKEHLPQFW K
//
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