ID T0I334_9SPHN Unreviewed; 260 AA.
AC T0I334;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Histidinol-phosphate phosphatase {ECO:0000313|EMBL:EQB18798.1};
GN ORFNames=L284_03785 {ECO:0000313|EMBL:EQB18798.1};
OS Novosphingobium lindaniclasticum LE124.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB18798.1, ECO:0000313|Proteomes:UP000015527};
RN [1] {ECO:0000313|EMBL:EQB18798.1, ECO:0000313|Proteomes:UP000015527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LE124 {ECO:0000313|EMBL:EQB18798.1,
RC ECO:0000313|Proteomes:UP000015527};
RX PubMed=24029761;
RA Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT a Hexachlorocyclohexane Dumpsite.";
RL Genome Announc. 1:e00715-13(2013).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759}.
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:EQB18798.1}.
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; ATHL01000032; EQB18798.1; -; Genomic_DNA.
DR RefSeq; WP_021232724.1; NZ_ATHL01000032.1.
DR AlphaFoldDB; T0I334; -.
DR PATRIC; fig|1096930.3.peg.745; -.
DR eggNOG; COG0483; Bacteria.
DR OrthoDB; 9785695at2; -.
DR Proteomes; UP000015527; Unassembled WGS sequence.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01641; Bacterial_IMPase_like_1; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR InterPro; IPR011809; His_9_proposed.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR NCBIfam; TIGR02067; his_9_HisN; 1.
DR PANTHER; PTHR43200:SF26; BIFUNCTIONAL PHOSPHATASE IMPL2, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43200; PHOSPHATASE; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000015527}.
SQ SEQUENCE 260 AA; 27869 MW; 7BE4BC5EC7BA47DE CRC64;
MKLDNDIALA LRLADAAGEA IRPHFRSGVG VERKGDASPV TVADRAAEEA IRRILKAEVP
RDGVIGEEFG SEEGSSNRTW VLDPIDGTVS FIAGRPIFGT LIALLVDGWP VLGVIDQPIL
GERWVGASGF ATTFNGKEVR TRACRELSDA MLATTGPHYF DDHQGEHFMA LAAKTDHKRM
VMGGDCYNYG LLASGHLDVV CEAGLKLHDW AALVPIVEGA GGTMCDWNGE PLHAQSDGHI
LALGDPARLE DVVDALDCHH
//
