ID K1L371_9BACT Unreviewed; 287 AA.
AC K1L371;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 Name=hisK {ECO:0000313|EMBL:EKB50840.1};
GN ORFNames=B879_00585 {ECO:0000313|EMBL:EKB50840.1};
OS Cecembia lonarensis LW9.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cecembia.
OX NCBI_TaxID=1225176 {ECO:0000313|EMBL:EKB50840.1, ECO:0000313|Proteomes:UP000004478};
RN [1] {ECO:0000313|EMBL:EKB50840.1, ECO:0000313|Proteomes:UP000004478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LW9 {ECO:0000313|EMBL:EKB50840.1,
RC ECO:0000313|Proteomes:UP000004478};
RX PubMed=23144386; DOI=10.1128/JB.01729-12;
RA Shivaji S., Ara S., Singh A., Pinnaka A.K.;
RT "Draft Genome Sequence of Cecembia lonarensis Strain LW9T, Isolated from
RT Lonar Lake, a Haloalkaline Lake in India.";
RL J. Bacteriol. 194:6631-6631(2012).
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:EKB50840.1}.
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DR EMBL; AMGM01000005; EKB50840.1; -; Genomic_DNA.
DR RefSeq; WP_009183634.1; NZ_AMGM01000005.1.
DR AlphaFoldDB; K1L371; -.
DR OrthoDB; 9775255at2; -.
DR UniPathway; UPA00031; UER00013.
DR Proteomes; UP000004478; 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 CDD; cd12110; PHP_HisPPase_Hisj_like; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR010140; Histidinol_P_phosphatase_HisJ.
DR InterPro; IPR004013; PHP_dom.
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 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:UP000004478}.
FT DOMAIN 6..208
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
SQ SEQUENCE 287 AA; 33552 MW; F087358725CF3C37 CRC64;
MSWTNYHSHY KYCDGVDEID SHVQKALELG IKSFGFTSHS PVHFENKWSM DSKDLPTYLK
EVDHAKTKYA GQIEIYKSLE IDYFPEKTGI IKAFRKDLKL DYTLGSIHFI DAFEDGKPWE
IDGPQLVFEK GLQEIYGNDI QKVLRRYFEI TVHMLEHDCP NILGHMDKIK MQNHNKFFFD
EEATWYKDYL SQTLEVAAQA GTIVEVNTRG LYKKRASETY PGKFGLQRLK ELKVPICLNS
DSHHPKEIIG EYENTVLLLK ELGFRELMVL KDNVWIARPF DQSGINW
//