ID A0A060US06_9PROT Unreviewed; 265 AA.
AC A0A060US06;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN Name=suhB {ECO:0000313|EMBL:CDQ11215.1};
GN ORFNames=AFERRI_530110 {ECO:0000313|EMBL:CDQ11215.1}, H2515_10510
GN {ECO:0000313|EMBL:QQD71861.1};
OS Acidithiobacillus ferrivorans.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=160808 {ECO:0000313|EMBL:CDQ11215.1, ECO:0000313|Proteomes:UP000029069};
RN [1] {ECO:0000313|EMBL:CDQ11215.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF27 {ECO:0000313|EMBL:CDQ11215.1};
RA Genoscope - CEA;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDQ11215.1, ECO:0000313|Proteomes:UP000029069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF27 {ECO:0000313|EMBL:CDQ11215.1,
RC ECO:0000313|Proteomes:UP000029069};
RA Talla E., Hedrich S., Mangenot S., Ji B., Johnson D.B., Barbe V.,
RA Bonnefoy V.;
RT "Initial genome analysis of the psychrotolerant acidophile
RT Acidithiobacillus ferrivorans CF27: insights into iron and sulfur oxidation
RT pathways and into biofilm formation.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QQD71861.1, ECO:0000313|Proteomes:UP000595420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XJFY6S-08 {ECO:0000313|EMBL:QQD71861.1,
RC ECO:0000313|Proteomes:UP000595420};
RA Yan L., Ni Y.;
RT "Complete genome sequence analysis of Acidithiobacillus ferrivorans XJFY6S-
RT 08 reveals extreme environmental adaptation to alpine acid mine drainage.";
RL Submitted (JUL-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC Evidence={ECO:0000256|ARBA:ARBA00001033,
CC ECO:0000256|RuleBase:RU364068};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU364068};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}.
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; CCCS020000049; CDQ11215.1; -; Genomic_DNA.
DR EMBL; CP059488; QQD71861.1; -; Genomic_DNA.
DR RefSeq; WP_035194140.1; NZ_LT841305.1.
DR AlphaFoldDB; A0A060US06; -.
DR Proteomes; UP000029069; Unassembled WGS sequence.
DR Proteomes; UP000595420; Chromosome.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR CDD; cd01639; IMPase; 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; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR InterPro; IPR022337; Inositol_monophosphatase_SuhB.
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 PRINTS; PR01959; SBIMPHPHTASE.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364068};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364068};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364068}.
SQ SEQUENCE 265 AA; 29410 MW; 73EDDCB98A6CCCFC CRC64;
MQHPILVTAI RAARKAGDII NRSFDRVNEI SITTKAHNDF VTDVDQRAEA AIVEIVRRAY
PDHGILAEEG SRISDKDFEW IIDPLDGTTN FIHGMPQLCV SIAVRHFDRL EHAVIYNPVH
DELFTASRGS GAHLNDRRLR IAQRKDLDGA LLGTGFPFRD FSYLDTYLAT FKALMLKTAG
IRRPGSAALD LAYVAAGRYD GFWEFNLKPW DIAAGALLVQ EAGGVATDFK GDQSYLQNGN
IVAGNLRIHA QMLHIISQEI NKPAS
//
