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Multifunctional fusion protein [Includes: Deoxyribose-phosphate aldolase (DERA) (EC 4.1.2.4) (2-deoxy-D-ribose 5-phosphate aldolase) (Phosphodeoxyriboaldolase) (Deoxyriboaldolase); Phosphopentomutase (EC 5.4.2.7) (Phosphodeoxyribomutase)]

 W0FLJ6_9BACT            Unreviewed;       611 AA.
W0FLJ6;
19-MAR-2014, integrated into UniProtKB/TrEMBL.
19-MAR-2014, sequence version 1.
22-NOV-2017, entry version 29.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00114, ECO:0000256|HAMAP-Rule:MF_00740};
Includes:
RecName: Full=Deoxyribose-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
Short=DERA {ECO:0000256|HAMAP-Rule:MF_00114};
EC=4.1.2.4 {ECO:0000256|HAMAP-Rule:MF_00114};
AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase {ECO:0000256|HAMAP-Rule:MF_00114};
AltName: Full=Phosphodeoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
Short=Deoxyriboaldolase {ECO:0000256|HAMAP-Rule:MF_00114};
Includes:
RecName: Full=Phosphopentomutase {ECO:0000256|HAMAP-Rule:MF_00740};
EC=5.4.2.7 {ECO:0000256|HAMAP-Rule:MF_00740};
AltName: Full=Phosphodeoxyribomutase {ECO:0000256|HAMAP-Rule:MF_00740};
Name=deoC {ECO:0000256|HAMAP-Rule:MF_00114};
Synonyms=deoB {ECO:0000256|HAMAP-Rule:MF_00740};
uncultured bacterium Contig1532b.
Bacteria; environmental samples.
NCBI_TaxID=1393450 {ECO:0000313|EMBL:AHF23687.1};
[1] {ECO:0000313|EMBL:AHF23687.1}
NUCLEOTIDE SEQUENCE.
PubMed=24223817;
Wang L., Hatem A., Catalyurek U.V., Morrison M., Yu Z.;
"Metagenomic insights into the carbohydrate-active enzymes carried by
the microorganisms adhering to solid digesta in the rumen of cows.";
PLoS ONE 8:E78507-E78507(2013).
-!- FUNCTION: Catalyzes a reversible aldol reaction between
acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-
D-ribose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00114}.
-!- FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of
pentose. {ECO:0000256|HAMAP-Rule:MF_00740,
ECO:0000256|SAAS:SAAS00847417}.
-!- CATALYTIC ACTIVITY: 2-deoxy-D-ribose 5-phosphate = D-
glyceraldehyde 3-phosphate + acetaldehyde. {ECO:0000256|HAMAP-
Rule:MF_00114}.
-!- CATALYTIC ACTIVITY: 2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-
alpha-D-ribose 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00740,
ECO:0000256|SAAS:SAAS00847419}.
-!- CATALYTIC ACTIVITY: Alpha-D-ribose 1-phosphate = D-ribose 5-
phosphate. {ECO:0000256|HAMAP-Rule:MF_00740,
ECO:0000256|SAAS:SAAS00847422}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000256|HAMAP-Rule:MF_00740};
Note=Binds 1 or 2 manganese ions. {ECO:0000256|HAMAP-
Rule:MF_00740};
-!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
deoxy-alpha-D-ribose 1-phosphate: step 2/2. {ECO:0000256|HAMAP-
Rule:MF_00114}.
-!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-
ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-
diphosphate from D-ribose 5-phosphate (route II): step 1/3.
{ECO:0000256|HAMAP-Rule:MF_00740, ECO:0000256|SAAS:SAAS00847418}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00740,
ECO:0000256|SAAS:SAAS00847414}.
-!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 1
subfamily. {ECO:0000256|HAMAP-Rule:MF_00114}.
-!- SIMILARITY: Belongs to the phosphopentomutase family.
{ECO:0000256|HAMAP-Rule:MF_00740, ECO:0000256|SAAS:SAAS00851403}.
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EMBL; KC246771; AHF23687.1; -; Genomic_DNA.
UniPathway; UPA00002; UER00468.
UniPathway; UPA00087; UER00173.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-UniRule.
GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
GO; GO:0009264; P:deoxyribonucleotide catabolic process; IEA:UniProtKB-UniRule.
GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
CDD; cd00959; DeoC; 1.
CDD; cd16009; PPM; 1.
Gene3D; 3.20.20.70; -; 1.
Gene3D; 3.30.70.1250; -; 1.
Gene3D; 3.40.720.10; -; 1.
HAMAP; MF_00114; DeoC_type1; 1.
HAMAP; MF_00740; Phosphopentomut; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR017850; Alkaline_phosphatase_core_sf.
InterPro; IPR010045; DeoB.
InterPro; IPR011343; DeoC.
InterPro; IPR002915; DeoC/FbaB/lacD_aldolase.
InterPro; IPR028581; DeoC_typeI.
InterPro; IPR006124; Metalloenzyme.
InterPro; IPR024052; Phosphopentomutase_DeoB_cap_sf.
PANTHER; PTHR21110; PTHR21110; 1.
Pfam; PF01791; DeoC; 1.
Pfam; PF01676; Metalloenzyme; 1.
SMART; SM01133; DeoC; 1.
SUPFAM; SSF143856; SSF143856; 1.
SUPFAM; SSF53649; SSF53649; 2.
TIGRFAMs; TIGR01696; deoB; 1.
TIGRFAMs; TIGR00126; deoC; 1.
3: Inferred from homology;
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00740,
ECO:0000256|SAAS:SAAS00847416};
Isomerase {ECO:0000256|HAMAP-Rule:MF_00740,
ECO:0000256|SAAS:SAAS00847411};
Lyase {ECO:0000256|HAMAP-Rule:MF_00114};
Manganese {ECO:0000256|HAMAP-Rule:MF_00740,
ECO:0000256|SAAS:SAAS00456930};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00740,
ECO:0000256|SAAS:SAAS00456876};
Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
DOMAIN 3 381 Metalloenzyme.
{ECO:0000259|Pfam:PF01676}.
ACT_SITE 491 491 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00114}.
ACT_SITE 555 555 Schiff-base intermediate with
acetaldehyde. {ECO:0000256|HAMAP-
Rule:MF_00114}.
ACT_SITE 584 584 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00114}.
METAL 11 11 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
METAL 299 299 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
METAL 335 335 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
METAL 336 336 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
METAL 347 347 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
SEQUENCE 611 AA; 65770 MW; 49872CD062DC4B71 CRC64;
MAKRVFLIIL DSLGCGNAPD ASAFGDQGSN TLAAVLSASD KPFPNLSSMG LFDIDGNSDP
RILEYLSKDP QAGRPAPIGA YGRLREESSG GKDSTIGHWE IAGVVSEDPQ PTYPDGFPSY
VVDKLKEISG RGVLCNLPYS GTQAIEDYGE EHFSSGDLIL YTSADSVLQI AAHEEIVPLD
ELYRICREMR TFMTGKDAVG RIIARPFTGT PGSFTRTANR HDFAVEAPSA TMMDHLKAKG
FDVISVGKIY DLFAGRGFTE TNPTKGNSEG IAKIREYLDK DFTGLLFSNL VDFDMLYGHR
NNIEGYNEAL HEFDDALGDI LESLKEDDLL IISADHGCDP STVSTDHSRE QVPLLIYGKG
YSTPRNLGSI TGFSYISQVV VNALSGARFE KRFPERDLDP SDPGDVMTYV DLTNLKVTAT
EDDIKALIDR AIASKTMSVC IPPCYVRSAY DYARGRIPIC TVIGFPNGYN TTSVKVTEAK
DAVDNGACEI DMVINVAFVK AGKMKEVEDE VKAIAGAVHE KGAILKVIIE ACLLTEEEKV
ALCGIVERCG AEYIKTSTGF STGGATVEDV ALMRANLSSS VRIKAAGGIR SPEAARAMID
AGATRIGASG L


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