ID L0KIK1_MESAW Unreviewed; 456 AA.
AC L0KIK1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Family 4 glycosyl hydrolase, alpha-galactosidase/6-phospho-beta-glucosidase {ECO:0000313|EMBL:AGB44821.1};
GN OrderedLocusNames=Mesau_02392 {ECO:0000313|EMBL:AGB44821.1};
OS Mesorhizobium australicum (strain HAMBI 3006 / LMG 24608 / WSM2073).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=754035 {ECO:0000313|EMBL:AGB44821.1, ECO:0000313|Proteomes:UP000010998};
RN [1] {ECO:0000313|Proteomes:UP000010998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24608 / HAMBI 3006 / WSM2073
RC {ECO:0000313|Proteomes:UP000010998};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Gu W., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Reeve W.G., Howieson J.G., Tiwari R.P.,
RA O'Hara G.W., Atkins C.A., Ronson C.W., Nandasena K.G., Woyke T.;
RT "Complete sequence of Mesorhizobium australicum WSM2073.";
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; CP003358; AGB44821.1; -; Genomic_DNA.
DR RefSeq; WP_015316262.1; NC_019973.1.
DR AlphaFoldDB; L0KIK1; -.
DR STRING; 754035.Mesau_02392; -.
DR KEGG; mam:Mesau_02392; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_1_1_5; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000010998; Chromosome.
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:UP000010998}.
FT DOMAIN 199..419
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 456 AA; 51499 MW; AE6A24448EAF3069 CRC64;
MARHPRITFI GAGSTVFMKN IVGDVLQRPA LSGATIALMD INPQRLEESA VVVNKLIATL
GVKAMAETYT DQRKALADAD FVVVAFQIGG YEPCTVTDFE VPKTYGLRQT IADTLGVGGI
MRGLRTVPHL WKICEDMLAV CPRAIMLQYV NPMAINTWAI SEKYPEIRQV GLCHSVQGTA
MELAHDLDLP YDEIRYRSAG INHMAFYLQF EHRQPDGSYR DLYPDLVRAY REGRAPKPGW
NPRCPNKVRY EMLTRLGYFV TESSEHFAEY TPYFIKDGRP DLIEKYGIPL DEYPKRCVEQ
IERWKDQAQA YRSAQRIEVE ESKEYASSIM NSVWTGEPSV IYGNVRNNGC ITSLPRDCAA
EVPCLVDASG IQPIYIGDLP PQLTALIRTN INVQELTVRA LMSENREHIY HAAMMDPHTA
AELDLDQIWS LVDDLLAAHG DWLPAWARVK RKNEAA
//
