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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)]

 A0A1W1YNF2_9FIRM        Unreviewed;       610 AA.
A0A1W1YNF2;
07-JUN-2017, integrated into UniProtKB/TrEMBL.
07-JUN-2017, sequence version 1.
22-NOV-2017, entry version 5.
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=deoB {ECO:0000256|HAMAP-Rule:MF_00740};
Synonyms=deoC {ECO:0000256|HAMAP-Rule:MF_00114};
ORFNames=SAMN06296952_0813 {ECO:0000313|EMBL:SMC37689.1};
Ruminococcaceae bacterium.
Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
unclassified Ruminococcaceae.
NCBI_TaxID=1898205 {ECO:0000313|EMBL:SMC37689.1, ECO:0000313|Proteomes:UP000192633};
[1] {ECO:0000313|EMBL:SMC37689.1, ECO:0000313|Proteomes:UP000192633}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KHP2 {ECO:0000313|EMBL:SMC37689.1,
ECO:0000313|Proteomes:UP000192633};
Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
Dimitrov K.M., Suarez D.L., Swayne D.E.;
Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
-!- 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; FWXP01000002; SMC37689.1; -; Genomic_DNA.
UniPathway; UPA00002; UER00468.
UniPathway; UPA00087; UER00173.
Proteomes; UP000192633; Unassembled WGS sequence.
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;
Complete proteome {ECO:0000313|Proteomes:UP000192633};
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};
Reference proteome {ECO:0000313|Proteomes:UP000192633};
Schiff base {ECO:0000256|HAMAP-Rule:MF_00114}.
DOMAIN 3 366 Metalloenzyme.
{ECO:0000259|Pfam:PF01676}.
ACT_SITE 489 489 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00114}.
ACT_SITE 553 553 Schiff-base intermediate with
acetaldehyde. {ECO:0000256|HAMAP-
Rule:MF_00114}.
ACT_SITE 582 582 Proton donor/acceptor.
{ECO:0000256|HAMAP-Rule:MF_00114}.
METAL 11 11 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
METAL 296 296 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
METAL 332 332 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
METAL 333 333 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
METAL 344 344 Manganese. {ECO:0000256|HAMAP-
Rule:MF_00740}.
SEQUENCE 610 AA; 66070 MW; 110A76231C7983ED CRC64;
MAKRVFLVVL DSFGIGLAPD AERFGDKGSN TLAAVCSYGN EPFENLTKMG LFDIDGHDDK
RIRDYIAAQT DMPAPIGSYG RIRELSDGKD STIGHWEMAG VLSSRPLPTY PDGFPQEIID
ELKEKTGRDI ICNKPYSGTE VIKDYGEEHM KTGALIVYTS ADSVLQIAAH EDVVPVEELY
GYCKIARDIM KGEHAVGRVI ARPFEGVPGN FTRTPRRHDF SLEAPAATLP DIVKAAGLDV
ISVGKINDLF AGRGMTKTNP TSGNTEGIKK MLEYVDKDFN GLCYINLVDF DMKYGHRNDI
EGYNKAMHEF DEALGKMISL LYPDDLLIVT ADHGCDPSTE STDHSRETVP VLIYGEGHNV
PHNMGTLAGF THVADIAFDA LLAAPYKREF TPAVGANIPD PDNIMSRVDM TNLKVTATED
DIKDLVKRAI EAKAASVCVQ PCYVRLASKE AKGKMSICTV IGFPNGYNTT SVKKFEAEEA
CDNGASEIDM VINQCMLKSG DINAVGAEIG VIAEAVHAKG AILKVIIETC NLTRKEKAVL
CHIVTVQGAD FIKTSTGFGS AGATLEDVSY MRRMCGGDVR VKAAGGIRTK EDAQKMVEAG
ADRIGASALK


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