ID Q1ZA38_9GAMM Unreviewed; 451 AA.
AC Q1ZA38;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE SubName: Full=Putative alpha-galactosidase {ECO:0000313|EMBL:EAS45654.1};
GN ORFNames=P3TCK_04736 {ECO:0000313|EMBL:EAS45654.1};
OS Photobacterium profundum 3TCK.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314280 {ECO:0000313|EMBL:EAS45654.1, ECO:0000313|Proteomes:UP000003789};
RN [1] {ECO:0000313|EMBL:EAS45654.1, ECO:0000313|Proteomes:UP000003789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3TCK {ECO:0000313|EMBL:EAS45654.1,
RC ECO:0000313|Proteomes:UP000003789};
RA Bartlett D.H., Valle G., Lauro F.M., Vezzi A., Simonato F., Eloe E.,
RA Vitulo N., Stratton T.K., D'angelo M., Ferriera S., Johnson J., Kravitz S.,
RA Beeson K., Sutton G., Rogers Y., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2006) 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:EAS45654.1}.
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; AAPH01000001; EAS45654.1; -; Genomic_DNA.
DR RefSeq; WP_006228956.1; NZ_CH724134.1.
DR AlphaFoldDB; Q1ZA38; -.
DR HOGENOM; CLU_045951_1_1_6; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000003789; 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}.
FT DOMAIN 197..420
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 112
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 451 AA; 50861 MW; 2AE31F91534AE91F CRC64;
MKTPQITFIG AGSTIFVKNI LGDVFHKPAL KHAHIALMDI DQTRLEESQI VVRKLMESAG
ATGNITCHLN QKDALQDADF VVVAFQIGGY EPCTVTDFEV CKRHGLEQTI ADTLGPGGIM
RSLRTIPHLW QICEDMTEVC PDATMLNYVN PMAMNTWAMY AKYPNIKQVG LCHSVQGTAE
ELARDLELDY NDLRYTCAGI NHMAYYLTLE KKNAQGEYVD IYPDLLAAFE NGQAPKPGQH
HNGRCVNLIR YEMFKKLGYF VTESSEHFSE YTPYFIKPNR PDLIERYKVP LDEYPKRCVE
QIADWKQDLE AFKNADSIDV KESHEYASTI MNAIWTGTPS VIYGNVRNDG LIENLPQECC
VEVACLVDAN GIQPTKVGRL PSHLAALMQT NINVQTLLTE AILTENRDRI YHAAMLDPHT
AAVLGLEEIY TLVDDLIEAH EGWLPAWVHK H
//
