ID G2LQ22_BUCUM Unreviewed; 407 AA.
AC G2LQ22;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 13-SEP-2023, entry version 64.
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 ECO:0000313|EMBL:AEO08309.1};
GN ORFNames=BUAMB_516 {ECO:0000313|EMBL:AEO08309.1};
OS Buchnera aphidicola str. Ua (Uroleucon ambrosiae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=1005057 {ECO:0000313|EMBL:AEO08309.1, ECO:0000313|Proteomes:UP000006139};
RN [1] {ECO:0000313|EMBL:AEO08309.1, ECO:0000313|Proteomes:UP000006139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ua {ECO:0000313|EMBL:AEO08309.1,
RC ECO:0000313|Proteomes:UP000006139};
RX PubMed=21912528; DOI=10.1371/journal.pgen.1002252;
RA Degnan P.H., Ochman H., Moran N.A.;
RT "Sequence conservation and functional constraint on intergenic spacers in
RT reduced genomes of the obligate symbiont buchnera.";
RL PLoS Genet. 7:E1002252-E1002252(2011).
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}.
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DR EMBL; CP002648; AEO08309.1; -; Genomic_DNA.
DR RefSeq; WP_014500211.1; NC_017259.1.
DR AlphaFoldDB; G2LQ22; -.
DR STRING; 1005057.BUAMB_516; -.
DR KEGG; buh:BUAMB_516; -.
DR PATRIC; fig|1005057.4.peg.494; -.
DR eggNOG; COG1015; Bacteria.
DR HOGENOM; CLU_053861_0_0_6; -.
DR OrthoDB; 9769930at2; -.
DR UniPathway; UPA00087; UER00173.
DR Proteomes; UP000006139; Chromosome.
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};
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}.
FT DOMAIN 2..398
FT /note="Metalloenzyme"
FT /evidence="ECO:0000259|Pfam:PF01676"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT BINDING 311
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT BINDING 347
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT BINDING 348
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
FT BINDING 359
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740"
SQ SEQUENCE 407 AA; 45596 MW; D25A01BE9BF3A25A CRC64;
MKRIFLIVLD SFGIGFSSDA YKFNDVGANT FAHIVEKCFL GQADINRKGA LYIPNLIKLG
ITHAARAASK KKLLGYNNNL NVIGSYGFAS EISSGKDTTS GHWEMVGVPV LDNWCYFTNK
NNSFPKDILN YIICSSKLTG CLGNCHASGT DIISDLGEEH IRTKKPIIYT SSDSVLQIAC
HEVFFGLSNL YTLCKNIRIF LDKNKYKVAR VIARPFIGHK KSDFQRTGNR RDFSMKPFST
TVMQKLIDEK KGQVIAIGKV SDIYSGVGIS KHIKSTGLNE LCHNTIEEIK KSKNNTMVFT
NLVDFDSNWG HRRDVAGYAK GLEFFDKKLS QIIDLVQAND ILILTADHGC DPTWTGTDHT
RENVPILMYS PNLEKKFLGH RKTFADIGQT IAKYFLLSNM SYGESMF
//
