PNCB_BRADU
ID PNCB_BRADU Reviewed; 434 AA.
AC Q89SS3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00570};
DE Short=NAPRTase {ECO:0000255|HAMAP-Rule:MF_00570};
DE EC=6.3.4.21 {ECO:0000255|HAMAP-Rule:MF_00570};
GN Name=pncB {ECO:0000255|HAMAP-Rule:MF_00570}; OrderedLocusNames=bll2327;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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:0000255|HAMAP-Rule:MF_00570}.
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:0000255|HAMAP-
CC Rule:MF_00570};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00570}.
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:0000255|HAMAP-Rule:MF_00570}.
CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000255|HAMAP-
CC Rule:MF_00570}.
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DR EMBL; BA000040; BAC47592.1; -; Genomic_DNA.
DR RefSeq; NP_768967.1; NC_004463.1.
DR RefSeq; WP_011085115.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89SS3; -.
DR SMR; Q89SS3; -.
DR STRING; 224911.27350582; -.
DR EnsemblBacteria; BAC47592; BAC47592; BAC47592.
DR GeneID; 64022070; -.
DR KEGG; bja:bll2327; -.
DR PATRIC; fig|224911.44.peg.1874; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_030991_1_0_5; -.
DR InParanoid; Q89SS3; -.
DR OMA; QAVFHRY; -.
DR PhylomeDB; Q89SS3; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
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 PANTHER; PTHR11098; PTHR11098; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR01514; NAPRTase; 1.
PE 3: Inferred from homology;
KW Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW Reference proteome.
FT CHAIN 1..434
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_1000146832"
FT MOD_RES 242
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ SEQUENCE 434 AA; 49902 MW; 8EC682BBC4396356 CRC64;
MTVTDIASRT YNHSWRLDPI IRSLLDTDFY KLLMLQMIRE DYSNQQVTFS VINRSRHVRL
AEIIDEGELR AQLDHARTIR FTKKELIWLA GNTFYGKTHM FSADFIRWLA EFRLPEYELR
KVEGQYELHF HGPWTHTTMW EIPALAILNE LRSRAAIKGR GRFELDVLYA RAKAKLWTKV
ERLRKLENLR LSDFGTRRRH GFLWQRWCVE AVKEGLGPSF IGTSNVLLAM DNDLEAIGTN
AHELPMVAAG LAKDDEELRW APYRILDQWR QTYGGNLLIA LPDAFGTKAF LRDAPEWVAD
WTGFRPDSAP PIQAGEEIIA WWEKKGRNPR DKLLVFSDAM DVGSIEETYH HFTGRVRLSF
GWGTNLTNDF VGCAPDGSFN LDPISLVCKV SSVDGHPAVK LSDNPEKATG LPSEIERYLR
VFGDVGRVRK PVLV