ID A0A0P9CKH8_9BACL Unreviewed; 390 AA.
AC A0A0P9CKH8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Phosphopentomutase {ECO:0000256|HAMAP-Rule:MF_00740};
DE EC=5.4.2.7 {ECO:0000256|HAMAP-Rule:MF_00740};
DE AltName: Full=Phosphodeoxyribomutase {ECO:0000256|HAMAP-Rule:MF_00740};
GN Name=deoB {ECO:0000256|HAMAP-Rule:MF_00740};
GN ORFNames=AN477_11960 {ECO:0000313|EMBL:KPV43520.1};
OS Alicyclobacillus ferrooxydans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV43520.1, ECO:0000313|Proteomes:UP000050482};
RN [1] {ECO:0000313|EMBL:KPV43520.1, ECO:0000313|Proteomes:UP000050482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-34 {ECO:0000313|EMBL:KPV43520.1,
RC ECO:0000313|Proteomes:UP000050482};
RA Hemp J.;
RT "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
CC pentose. {ECO:0000256|HAMAP-Rule:MF_00740}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-D-ribose 5-
CC phosphate; Xref=Rhea:RHEA:27658, ChEBI:CHEBI:57259,
CC ChEBI:CHEBI:62877; Evidence={ECO:0000256|HAMAP-Rule:MF_00740};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-ribose 1-phosphate = D-ribose 5-phosphate;
CC Xref=Rhea:RHEA:18793, ChEBI:CHEBI:57720, ChEBI:CHEBI:78346;
CC EC=5.4.2.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00740};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00740};
CC Note=Binds 1 or 2 manganese ions. {ECO:0000256|HAMAP-Rule:MF_00740};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route II): step 1/3. {ECO:0000256|HAMAP-
CC Rule:MF_00740}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00740}.
CC -!- SIMILARITY: Belongs to the phosphopentomutase family.
CC {ECO:0000256|ARBA:ARBA00010373, ECO:0000256|HAMAP-Rule:MF_00740}.
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:KPV43520.1}.
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DR EMBL; LJCO01000048; KPV43520.1; -; Genomic_DNA.
DR RefSeq; WP_054969389.1; NZ_LJCO01000048.1.
DR AlphaFoldDB; A0A0P9CKH8; -.
DR STRING; 471514.AN477_11960; -.
DR PATRIC; fig|471514.4.peg.773; -.
DR OrthoDB; 9769930at2; -.
DR UniPathway; UPA00087; UER00173.
DR Proteomes; UP000050482; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00740; Phosphopentomut; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR010045; DeoB.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR024052; Phosphopentomutase_DeoB_cap_sf.
DR NCBIfam; TIGR01696; deoB; 1.
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.
DR SUPFAM; SSF143856; DeoB insert domain-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00740};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00740, ECO:0000313|EMBL:KPV43520.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00740};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00740}; Reference proteome {ECO:0000313|Proteomes:UP000050482}.
FT DOMAIN 3..376
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT BINDING 11
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT BINDING 324
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT BINDING 325
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT BINDING 336
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
SQ SEQUENCE 390 AA; 42368 MW; 04B2E097CEB33252 CRC64;
MSKRLIWIVL DSVGIGAAPD AQHYGHADEV SHTLLHIAQS VGGLKVPNLA RLGLGCIDEI
PGVECAGAKG AYGKMQERSF GKDTTNGHWE FVGVVLDQPM PVYPEGFPAH IIERFEEHVG
KRVLGNRPSS GTVILDELGE EHMKTGRPIV YTSADSVFQI AAHEDIVPIE TLYEWCRYAR
AILTGPDGVG RVIARPFIGS PGHFKRTGNR KDFSLTFGET VLTRIAHAGY PVVGIGKIHD
IYGGEGITEA VHTEGNEDGM NQLAEVMDRV HEGVIYINLV DFDALYGHRN DPVGFAKAVE
SFDARLPEVL TRLTKDDLLC ITADHGCDPT APGTDHTREW VPLLLYSTRM SGVVNLGERD
TFADIGATVA EYFQVEGPPV GKSALSALHV
//
