ID A0A1E8EXT7_9CLOT Unreviewed; 493 AA.
AC A0A1E8EXT7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN Name=pncB2 {ECO:0000313|EMBL:OFI05601.1};
GN ORFNames=CLOACE_16070 {ECO:0000313|EMBL:OFI05601.1};
OS Clostridium acetireducens DSM 10703.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121290 {ECO:0000313|EMBL:OFI05601.1, ECO:0000313|Proteomes:UP000175744};
RN [1] {ECO:0000313|EMBL:OFI05601.1, ECO:0000313|Proteomes:UP000175744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10703 {ECO:0000313|EMBL:OFI05601.1,
RC ECO:0000313|Proteomes:UP000175744};
RA Poehlein A., Fluechter S., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium acetireducens DSM 10703.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC {ECO:0000256|RuleBase:RU365100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide +
CC phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:456216; EC=6.3.4.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001240,
CC ECO:0000256|RuleBase:RU365100};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
CC -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC cycle. Phosphorylation strongly increases the affinity for substrates
CC and increases the rate of nicotinate D-ribonucleotide production.
CC Dephosphorylation regenerates the low-affinity form of the enzyme,
CC leading to product release. {ECO:0000256|RuleBase:RU365100}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
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:OFI05601.1}.
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DR EMBL; LZFO01000023; OFI05601.1; -; Genomic_DNA.
DR RefSeq; WP_070110581.1; NZ_LZFO01000023.1.
DR AlphaFoldDB; A0A1E8EXT7; -.
DR STRING; 1121290.CLAOCE_16070; -.
DR PATRIC; fig|1121290.3.peg.1594; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000175744; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01570; NAPRTase_A; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR041619; NAPRTase_C.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR NCBIfam; TIGR01513; NAPRTase_put; 1.
DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17956; NAPRTase_C; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR SUPFAM; SSF54675; Nicotinate/Quinolinate PRTase N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:OFI05601.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365100};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU365100};
KW Reference proteome {ECO:0000313|Proteomes:UP000175744};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:OFI05601.1}.
FT DOMAIN 17..141
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 162..333
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 371..480
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 493 AA; 56355 MW; 3A91FA619E77A33E CRC64;
MEYIKNFNVR NQRNLTMLVD FYELTMGNGY LESSVGNKIS YFDMFFRRVP DHGGYCIMAG
VQQLIEYLSS LKFTEDDIDY LRSKNIFSEK FLDYLKNFEF TCDVWAIPEG NPVFPNEPLV
TVKGPAIQAQ FVETMILLTI NHQTLIATKA NRICRAAEGR PVMEFGSRRA QGYDGAIYGA
RAAVIGGCSA TACTIAEEMF GIPAAGTMAH SWIQLFDSEY ESFKAWVDVY PDNCILLVDT
YNVLKSGLPN AIKVFDEVLV PRGYRPKGIR IDSGDITYLT QKCREILDNA GYPDVEIIVS
NSLDEYIISD VLAQGATINS FGVGERLITA KSEPVFGGVY KLVAVEDDEG NIVPKIKISE
NEEKITNPAF KKIYRIYDNI ANKAVADLIT LNDEEIDVSK PLEIFDPVYT WKRRRFKNYY
VKQLMVKIFD KGKQVYESPN VSEIKKIVKE ETEKLWPEVL RFENPHHYYV DLSEKLWNLK
QDLLHDYSIV YED
//
