ID R5TZQ0_9BACE Unreviewed; 388 AA.
AC R5TZQ0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|HAMAP-Rule:MF_00570};
DE Short=NAPRTase {ECO:0000256|HAMAP-Rule:MF_00570};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|HAMAP-Rule:MF_00570};
GN Name=pncB {ECO:0000256|HAMAP-Rule:MF_00570};
GN ORFNames=BN759_00656 {ECO:0000313|EMBL:CCZ71240.1};
OS Bacteroides sp. CAG:702.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262747 {ECO:0000313|EMBL:CCZ71240.1, ECO:0000313|Proteomes:UP000017962};
RN [1] {ECO:0000313|EMBL:CCZ71240.1, ECO:0000313|Proteomes:UP000017962}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:702 {ECO:0000313|Proteomes:UP000017962};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide
CC from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of
CC ATP. {ECO:0000256|HAMAP-Rule:MF_00570, ECO:0000256|RuleBase:RU003838}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00570, ECO:0000256|RuleBase:RU003838};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|HAMAP-Rule:MF_00570,
CC ECO:0000256|RuleBase:RU003838}.
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|HAMAP-Rule:MF_00570,
CC ECO:0000256|RuleBase:RU003838}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|HAMAP-Rule:MF_00570,
CC ECO:0000256|RuleBase:RU003838}.
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:CCZ71240.1}.
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DR EMBL; CBAM010000215; CCZ71240.1; -; Genomic_DNA.
DR AlphaFoldDB; R5TZQ0; -.
DR STRING; 1262747.BN759_00656; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000017962; 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 Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR HAMAP; MF_00570; NAPRTase; 1.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR006406; Nic_PRibTrfase.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR NCBIfam; TIGR01514; NAPRTase; 1.
DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF04095; NAPRTase; 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:CCZ71240.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00570};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW Rule:MF_00570};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|HAMAP-Rule:MF_00570};
KW Reference proteome {ECO:0000313|Proteomes:UP000017962};
KW Transferase {ECO:0000313|EMBL:CCZ71240.1}.
FT DOMAIN 7..127
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 161..372
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT MOD_RES 211
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00570"
SQ SEQUENCE 388 AA; 45364 MW; 4A8B6AE5A24D3D1B CRC64;
MVIKTVLDTD LYKFTTSYAY IKLFPYAMGT FSFKDRDDTE YTEGFLNALK NEIHNLALVS
LRKEELEYMC SHCRFLPRVY WEWLFSFRFD PDKIHVYLDD ERHLHMEVTD LLYKVTLYEV
PLLAIISEIK NQFLNRIPDR QDIIARLSGK VSLSNTHHMP FSEFGTRRRF SFDVHETVVA
YLKEHARYCT GTSNCFLAMK YNLLPMGTHP HEWFMFHGAQ FGYKHANYMA LENWVNVYDG
DLGTALSDTY TSDAFLSNFS RKQAKLFDGV RCDSGDEFEF VEHLIARYKE LGIDPTTKTI
IFSNALDFEK ALHIFEYCQG KIRCSFGIGT NLTNDTGYTP SNIVMKLSRC KMNVNQEWRE
CVKLSDDMGK HMGSSKELDA CLYELRLK
//
