ID S0J7J8_9FIRM Unreviewed; 483 AA.
AC S0J7J8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
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 ORFNames=C805_02787 {ECO:0000313|EMBL:EOT24575.1};
OS Eubacterium sp. 14-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1235790 {ECO:0000313|EMBL:EOT24575.1, ECO:0000313|Proteomes:UP000014176};
RN [1] {ECO:0000313|EMBL:EOT24575.1, ECO:0000313|Proteomes:UP000014176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14-2 {ECO:0000313|EMBL:EOT24575.1,
RC ECO:0000313|Proteomes:UP000014176};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Eubacterium bacterium 14-2.";
RL Submitted (APR-2013) 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:EOT24575.1}.
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DR EMBL; ASSS01000010; EOT24575.1; -; Genomic_DNA.
DR RefSeq; WP_016215813.1; NZ_KE159568.1.
DR AlphaFoldDB; S0J7J8; -.
DR STRING; 1235790.C805_02787; -.
DR PATRIC; fig|1235790.3.peg.3012; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_025154_2_1_9; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000014176; 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:EOT24575.1};
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:UP000014176};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:EOT24575.1}.
FT DOMAIN 6..129
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 150..318
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 360..471
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 483 AA; 54153 MW; 5263EEA189A71EEC CRC64;
MKHLTLLTDL YELTMMQGYF KSGSNETVVF DAFYRTNPCN GGYAVCAGLE QIMEYIRDLH
FSAEDIDYLR ALGIFDEDFL EYLSAFRFSG DIYAIPEGTI IFPREPLLKV IAPIMEAQLI
ETAILNILNH QSLIATKAAR VCYAADGDSV MEFGLRRAQG PDAGVYGARA AVIGGCCGTS
NVLCGQMFDV PVKGTHAHSW IMSFPDEYTA FKKYAELYPS ACILLVDTYD TLTSGVPNAV
RVFTELREAG VPLTFYGIRM DSGDLAYLSK IVRRMLDEAG FPDAVISASN DLDEYLIETL
KAQGARITSW GVGTNLITSK DCPAFGGVYK LAAIQDEQGN FLPKIKLSEN TEKVTNPGNK
TVYRIYEKDS GKIKADLICL AGETFDTARD LRLFDSLETW KRTTLKAGSY TMRELLIPIF
KQGTCIYESP SVMEIQRYCN KEKETLWNET KRFANPHEVY VDLSDELFDM KRKILNKFST
EKQ
//
