ID B0N5D3_9FIRM Unreviewed; 277 AA.
AC B0N5D3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Histidinol-phosphatase {ECO:0000256|ARBA:ARBA00013085, ECO:0000256|RuleBase:RU366003};
DE Short=HolPase {ECO:0000256|RuleBase:RU366003};
DE EC=3.1.3.15 {ECO:0000256|ARBA:ARBA00013085, ECO:0000256|RuleBase:RU366003};
GN ORFNames=CLORAM_01847 {ECO:0000313|EMBL:EDS18301.1};
OS Thomasclavelia ramosa DSM 1402.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=445974 {ECO:0000313|EMBL:EDS18301.1, ECO:0000313|Proteomes:UP000005798};
RN [1] {ECO:0000313|EMBL:EDS18301.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS18301.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium ramosum(DSM 1402).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS18301.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS18301.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate;
CC Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001216,
CC ECO:0000256|RuleBase:RU366003};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC {ECO:0000256|ARBA:ARBA00004970, ECO:0000256|RuleBase:RU366003}.
CC -!- SIMILARITY: Belongs to the PHP hydrolase family. HisK subfamily.
CC {ECO:0000256|ARBA:ARBA00009152, ECO:0000256|RuleBase:RU366003}.
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:EDS18301.1}.
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DR EMBL; ABFX02000006; EDS18301.1; -; Genomic_DNA.
DR RefSeq; WP_003537499.1; NZ_DS499657.1.
DR AlphaFoldDB; B0N5D3; -.
DR GeneID; 64195529; -.
DR eggNOG; COG1387; Bacteria.
DR HOGENOM; CLU_054611_3_0_9; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000005798; Unassembled WGS sequence.
DR GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR010140; Histidinol_P_phosphatase_HisJ.
DR InterPro; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR NCBIfam; TIGR01856; hisJ_fam; 1.
DR PANTHER; PTHR21039; HISTIDINOL PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR21039:SF0; HISTIDINOL-PHOSPHATASE; 1.
DR Pfam; PF02811; PHP; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF89550; PHP domain-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU366003};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102,
KW ECO:0000256|RuleBase:RU366003};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366003};
KW Reference proteome {ECO:0000313|Proteomes:UP000005798}.
FT DOMAIN 3..97
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 277 AA; 33011 MW; 74DF5504363CFC54 CRC64;
MFCDYHVHTE YSDDSCYLME DVIRDAIVLG IKEICFTDHV DYGIKLDWDD PNLIIKENEK
TIANVNYPQY FQKIDSLTEK YCNQITIKKG MEFGIQMHTI DKFQKLFNKY PFDFIILSIH
QVENKEFWTN DFQAGLSEAE YYQRYYQEMY DVVRNYHDYS VLGHMDLIKR YDDKDGYDAF
NEHKEIITRI LKYIIEDGKG IELNTSSVRY GLDDLMPSRD IFQLYYDLGG RIITIGSDSH
EKVHLGAHIE TMKKDLKKIG FKEFCTFKQM KPIFHKL
//
