VLDH_STRHL
ID VLDH_STRHL Reviewed; 213 AA.
AC Q15JF8;
DT 31-JAN-2018, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Validoxylamine A 7'-phosphate phosphatase {ECO:0000303|PubMed:21766819};
DE EC=3.1.3.101 {ECO:0000269|PubMed:21766819};
DE AltName: Full=Phosphomutase {ECO:0000303|PubMed:16725283};
GN Name=vldH {ECO:0000303|PubMed:16725283};
GN ORFNames=SHL15_8003 {ECO:0000312|EMBL:ALO98980.1};
OS Streptomyces hygroscopicus subsp. limoneus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=264445;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405
RC {ECO:0000312|EMBL:ABC67272.1};
RX PubMed=16725283; DOI=10.1016/j.gene.2005.12.035;
RA Singh D., Seo M.J., Kwon H.J., Rajkarnikar A., Kim K.R., Kim S.O.,
RA Suh J.W.;
RT "Genetic localization and heterologous expression of validamycin
RT biosynthetic gene cluster isolated from Streptomyces hygroscopicus var.
RT limoneus KCCM 11405 (IFO 12704).";
RL Gene 376:13-23(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405
RC {ECO:0000312|EMBL:ALO98980.1, ECO:0000312|Proteomes:UP000057753};
RA Kim K.M.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RC STRAIN=ATCC 21432 / NBRC 12704 / KCTC 1717 / KCCM 11405;
RX PubMed=21766819; DOI=10.1021/ja203574u;
RA Asamizu S., Yang J., Almabruk K.H., Mahmud T.;
RT "Pseudoglycosyltransferase catalyzes nonglycosidic C-N coupling in
RT validamycin a biosynthesis.";
RL J. Am. Chem. Soc. 133:12124-12135(2011).
CC -!- FUNCTION: Involved in the biosynthesis of the antifungal agent
CC validamycin A (PubMed:16725283). Catalyzes the dephosphorylation of
CC validoxylamine A 7'-phosphate to yield validoxylamine A
CC (PubMed:21766819). VldH is also able to convert trehalose 6-phosphate
CC to trehalose (PubMed:21766819). {ECO:0000269|PubMed:16725283,
CC ECO:0000269|PubMed:21766819}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + validoxylamine A 7'-phosphate = phosphate +
CC validoxylamine A; Xref=Rhea:RHEA:49400, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:111504, ChEBI:CHEBI:111505;
CC EC=3.1.3.101; Evidence={ECO:0000269|PubMed:21766819};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P77625};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P77625};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P77625};
CC Note=Requires the presence of a divalent metal cation for activity. Can
CC use magnesium, manganese or cobalt. {ECO:0000250|UniProtKB:P77625};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; DQ223652; ABC67272.1; -; Genomic_DNA.
DR EMBL; CP013220; ALO98980.1; -; Genomic_DNA.
DR RefSeq; WP_058084461.1; NZ_CP013220.1.
DR AlphaFoldDB; Q15JF8; -.
DR SMR; Q15JF8; -.
DR EnsemblBacteria; ALO98980; ALO98980; SHL15_8003.
DR BioCyc; MetaCyc:MON-19690; -.
DR BRENDA; 3.1.3.101; 14504.
DR Proteomes; UP000057753; Chromosome II.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Cobalt; Hydrolase; Magnesium; Manganese;
KW Metal-binding.
FT CHAIN 1..213
FT /note="Validoxylamine A 7'-phosphate phosphatase"
FT /id="PRO_0000442791"
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT ACT_SITE 10
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT BINDING 8..10
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 8
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 10
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 107..108
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P77247"
FT BINDING 165
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P77247"
SQ SEQUENCE 213 AA; 22796 MW; EFDC2B51F021BF29 CRC64;
MYKVALFDLD GTLINSEHKN REAWARLFRR HGVPYDDSVL RSFTGRPAKE AMADHVASFA
GHSVDELCAE VAAYAALPDM PAAVTVDGAM ELLHQLQQMR VPLGVVTSGP RDYAESALTT
LGALQLLDVL ITADDVSRGK PDPEGYSTAC SALNVEPSQA IVFEDAPAGI LAAKRAGIFC
VGLTTTHDAE ALAEADVLLK DLTEVRWPHI GPS
