ID A0A150MEZ2_9BACI Unreviewed; 401 AA.
AC A0A150MEZ2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Phosphopentomutase like {ECO:0000313|EMBL:KYD23110.1};
DE EC=5.4.2.7 {ECO:0000313|EMBL:KYD23110.1};
GN ORFNames=B4135_0639 {ECO:0000313|EMBL:KYD23110.1};
OS Caldibacillus debilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldibacillus.
OX NCBI_TaxID=301148 {ECO:0000313|EMBL:KYD23110.1, ECO:0000313|Proteomes:UP000075683};
RN [1] {ECO:0000313|EMBL:KYD23110.1, ECO:0000313|Proteomes:UP000075683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4135 {ECO:0000313|EMBL:KYD23110.1,
RC ECO:0000313|Proteomes:UP000075683};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Draft Genome Sequences of Seven Thermophilic Sporeformers Isolated from
RT Foods.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the phosphopentomutase family.
CC {ECO:0000256|ARBA:ARBA00010373}.
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:KYD23110.1}.
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DR EMBL; LQYT01000002; KYD23110.1; -; Genomic_DNA.
DR RefSeq; WP_061567846.1; NZ_LQYT01000002.1.
DR AlphaFoldDB; A0A150MEZ2; -.
DR STRING; 301148.B4135_0639; -.
DR PATRIC; fig|301148.3.peg.1466; -.
DR OrthoDB; 9769930at2; -.
DR Proteomes; UP000075683; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
DR CDD; cd16009; PPM; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR Gene3D; 3.30.70.1250; Phosphopentomutase; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR010045; DeoB.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR024052; Phosphopentomutase_DeoB_cap_sf.
DR PANTHER; PTHR21110; PHOSPHOPENTOMUTASE; 1.
DR PANTHER; PTHR21110:SF0; PHOSPHOPENTOMUTASE; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001491; Ppentomutase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000313|EMBL:KYD23110.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 282..385
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
SQ SEQUENCE 401 AA; 44755 MW; D43A6A3AC242AE6D CRC64;
MGRMMLLVID SFGIGAMDDC RDYVPSDCRA NTYKHIREAK KDELNIPTLY RLGLGALVDG
KSAPETNAYG YSKLAHHGAD TYLGHQEIAG SCPKKSNKRL MKEVHGQIKQ ALEAHGYEVA
YPFSHCQVLL VNGAAVVADN LESSLGNIIN VTADLKKMTF DELKKIGRIV RENVDTSRVI
ALGGPYTSIE RILSCVKEKH KDQWGVDTPK AGVYGKGYMV YHMGYGVEID KQFPMIAAKH
GLKVYRLGKT ADVLHGTGPA EPIVNTTELL ARFSELYRKE EGNASFLVNI QETDLAGHAE
NVDWYCRLLN ETDQWLQDFI PQMREEDILI IMADHGNDPT IGHSNHTREY VPIFIVGKKV
KPVYIGMRET MADVGATLCD FYGLPKTKEG ESFLDLILDR N
//
