ID U1F1X5_9ACTN Unreviewed; 266 AA.
AC U1F1X5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Histidinol phosphatase {ECO:0000313|EMBL:OCT42513.1};
DE SubName: Full=Histidinol-phosphate phosphatase HisN {ECO:0000313|EMBL:ERF57947.1};
GN ORFNames=H641_02098 {ECO:0000313|EMBL:ERF57947.1}, L860_09695
GN {ECO:0000313|EMBL:OCT42513.1};
OS Cutibacterium granulosum DSM 20700.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Cutibacterium.
OX NCBI_TaxID=1160719 {ECO:0000313|EMBL:ERF57947.1, ECO:0000313|Proteomes:UP000016307};
RN [1] {ECO:0000313|EMBL:ERF57947.1, ECO:0000313|Proteomes:UP000016307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:ERF57947.1,
RC ECO:0000313|Proteomes:UP000016307};
RX PubMed=24053623; DOI=10.1186/1471-2164-14-640;
RA Mak T.N., Schmid M., Brzuszkiewicz E., Zeng G., Meyer R., Sfanos K.S.,
RA Brinkmann V., Meyer T.F., Bruggemann H.;
RT "Comparative genomics reveals distinct host-interacting traits of three
RT major human-associated propionibacteria.";
RL BMC Genomics 14:640-640(2013).
RN [2] {ECO:0000313|EMBL:OCT42513.1, ECO:0000313|Proteomes:UP000094467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20700 {ECO:0000313|EMBL:OCT42513.1,
RC ECO:0000313|Proteomes:UP000094467};
RA Jahns A.C., Eilers H., Alexeyev O.A.;
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:ERF57947.1}.
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DR EMBL; AOSS01000057; ERF57947.1; -; Genomic_DNA.
DR EMBL; JNBU01000017; OCT42513.1; -; Genomic_DNA.
DR RefSeq; WP_021103440.1; NZ_AOSS01000057.1.
DR AlphaFoldDB; U1F1X5; -.
DR PATRIC; fig|1160719.4.peg.399; -.
DR OrthoDB; 9772456at2; -.
DR Proteomes; UP000016307; Unassembled WGS sequence.
DR Proteomes; UP000094467; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR PANTHER; PTHR20854:SF50; NUS FACTOR SUHB; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000016307}.
SQ SEQUENCE 266 AA; 28386 MW; 131D5F2D2A364A2F CRC64;
MVNVLDDLAL AHRIADEADA LTLARFRASD LRIDHKADHS EVTDADLAVE DAARRIVAAA
RPGDAVHGEE RADTGSGPRR WIIDPIDGTA NYARGVPVWA TLIALAEGDE VVASVVSAPA
LHRRWWAARG HGAWAGGPCV DEGSPIHVST VSDLREAFLS YSSLHGWDES DRGDEFAKLM
ATVWRTRAFG DFWSYMLVAE GVVDLAAEPE LNLHDMAALD VIVREAGGTF TTVAGQPGPW
GPDALASNGL LHEQAMTILG SGAHTA
//