ID A0A1V4IKK6_9CLOT Unreviewed; 494 AA.
AC A0A1V4IKK6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:OPJ60466.1};
GN ORFNames=CLCHR_29520 {ECO:0000313|EMBL:OPJ60466.1}, D2A34_08870
GN {ECO:0000313|EMBL:RII35309.1}, GKZ28_00470
GN {ECO:0000313|EMBL:MVX62173.1};
OS Clostridium chromiireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=225345 {ECO:0000313|EMBL:OPJ60466.1, ECO:0000313|Proteomes:UP000191056};
RN [1] {ECO:0000313|EMBL:OPJ60466.1, ECO:0000313|Proteomes:UP000191056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23318 {ECO:0000313|EMBL:OPJ60466.1,
RC ECO:0000313|Proteomes:UP000191056};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium chromiireducens DSM 23318.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RII35309.1, ECO:0000313|Proteomes:UP000265930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C1 {ECO:0000313|EMBL:RII35309.1,
RC ECO:0000313|Proteomes:UP000265930};
RA Xing M., Wei Y., Ang E.L., Zhao H., Zhang Y.;
RT "Genome of Clostridium chromiireducens C1, DSM12136.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:MVX62173.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NM79_F5 {ECO:0000313|EMBL:MVX62173.1};
RA Navarre W., Wong E.;
RT "Microbes associate with the intestines of laboratory mice.";
RL Submitted (DEC-2019) 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:OPJ60466.1}.
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DR EMBL; WSRQ01000001; MVX62173.1; -; Genomic_DNA.
DR EMBL; MZGT01000039; OPJ60466.1; -; Genomic_DNA.
DR EMBL; QXDJ01000002; RII35309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4IKK6; -.
DR STRING; 225345.CLCHR_29520; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000191056; Unassembled WGS sequence.
DR Proteomes; UP000265930; Unassembled WGS sequence.
DR Proteomes; UP000656077; 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:OPJ60466.1};
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:UP000191056};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:OPJ60466.1}.
FT DOMAIN 17..141
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 162..330
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 370..479
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 494 AA; 56272 MW; B47171D4DF8F70EF CRC64;
MDNKPDFNVK DERNLTMLVD FYELTMGNGY FDKGLKDRIA YFDMFFRRVP DGGGYCIMAG
VEQLIDYLKS LKFTHDDITY LRSKQLFSEE FLEYLENFNF SCDVWAVPEG NPVFPNEPLV
TVRGPVIQAQ FLETMILLTI NHQTLIATKA NRICRAAEGR PVMEFGSRRA QGYDGAIYGA
RAAIIGGCSS TACTMSDRMF NIPAVGTMAH SWVQLYDTEY DAFKAWAEIY PDDCVLLIDT
YNVIKSGIPN SIKVFNEILK PLGKRPRGIR IDSGDITYLT TKCRQMLDEA GYPDCGIVVS
NSLDEHIIKD VLDQGACINS FGVGERLITA KSEPVFGGVY KLVALAGDNS IIPKIKISEN
EEKITNPGFK KIVRIFDKNS HKALADLIAL RDEHINENEP LVIFDPIHTW KRKKISNYYT
KDLQVQIFKS GQCIYESPSV LDIKEFSKTE TDKLWPEVLR FENPHTYYVD LSQNLWSLKH
SLLHKYTNSY ETQD
//
