ID I2BBP2_SHIBC Unreviewed; 272 AA.
AC I2BBP2; K6W1G7;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=HMP-PP phosphatase {ECO:0000256|HAMAP-Rule:MF_01847};
DE EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01847};
GN Name=cof {ECO:0000256|HAMAP-Rule:MF_01847,
GN ECO:0000313|EMBL:AFJ47946.1};
GN OrderedLocusNames=EBL_c28760 {ECO:0000313|EMBL:AFJ47946.1};
OS Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS CDC 9005-74) (Escherichia blattae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shimwellia.
OX NCBI_TaxID=630626 {ECO:0000313|EMBL:AFJ47946.1, ECO:0000313|Proteomes:UP000001955};
RN [1] {ECO:0000313|EMBL:AFJ47946.1, ECO:0000313|Proteomes:UP000001955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74
RC {ECO:0000313|Proteomes:UP000001955};
RX PubMed=22843577; DOI=10.1128/JB.00829-12;
RA Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT DSM 4481, isolated from a cockroach.";
RL J. Bacteriol. 194:4436-4436(2012).
CC -!- FUNCTION: Catalyzes the hydrolysis of 4-amino-2-methyl-5-
CC hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-
CC hydroxymethylpyrimidine phosphate (HMP-P). {ECO:0000256|HAMAP-
CC Rule:MF_01847}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + H2O = 4-
CC amino-2-methyl-5-(phosphooxymethyl)pyrimidine + H(+) + phosphate;
CC Xref=Rhea:RHEA:27914, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57841, ChEBI:CHEBI:58354;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01847};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01847};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC {ECO:0000256|HAMAP-Rule:MF_01847}.
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DR EMBL; CP001560; AFJ47946.1; -; Genomic_DNA.
DR RefSeq; WP_002444597.1; NZ_BAHA01000034.1.
DR AlphaFoldDB; I2BBP2; -.
DR STRING; 630626.EBL_c28760; -.
DR KEGG; ebt:EBL_c28760; -.
DR PATRIC; fig|630626.3.peg.2792; -.
DR eggNOG; COG0561; Bacteria.
DR HOGENOM; CLU_044146_5_2_6; -.
DR OrthoDB; 5498330at2; -.
DR Proteomes; UP000001955; Chromosome.
DR GO; GO:0002145; F:4-amino-5-hydroxymethyl-2-methylpyrimidine diphosphatase activity; IEA:RHEA.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR CDD; cd07516; HAD_Pase; 1.
DR Gene3D; 3.30.1240.10; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR HAMAP; MF_01847; HMP_PP_phosphat; 1.
DR InterPro; IPR000150; Cof.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023938; HMP-PP_phosphatase.
DR NCBIfam; TIGR00099; Cof-subfamily; 1.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR PANTHER; PTHR47267; -; 1.
DR PANTHER; PTHR47267:SF2; HMP-PP PHOSPHATASE; 1.
DR Pfam; PF08282; Hydrolase_3; 1.
DR SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS01228; COF_1; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01847};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01847};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01847}; Reference proteome {ECO:0000313|Proteomes:UP000001955}.
FT ACT_SITE 8
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01847"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01847"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01847"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01847"
SQ SEQUENCE 272 AA; 30165 MW; 5391B93AB39D5A82 CRC64;
MTQLVAFDMD GTLLMPDHRP GDETLRTLGR LRERGITLTF ATGRHILEMQ PLLRRFGLSG
WLITGNGTRI HSASGEPLFR CDLAPEVAES VLHSHWDTRA SMHVFNDSGW LTDKPLPELL
KAHGYSGFQY QLADLRRLSA HEVTKICFCG DHEDLCQLRI ALQEQLGDSA AVCFSAVDCL
EVLPHNCNKG TALRALSERL AIPLRECMAF GDAMNDQEML SCVGRGVIMG NAMPQLIQSL
PQLPVIGHCA GQAIAHYLTH WLDTPHLSYS PE
//
