PNCB_RHILO
ID PNCB_RHILO Reviewed; 434 AA.
AC Q98D24;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 116.
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=mll4892;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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; BA000012; BAB51447.1; -; Genomic_DNA.
DR RefSeq; WP_010912788.1; NC_002678.2.
DR AlphaFoldDB; Q98D24; -.
DR SMR; Q98D24; -.
DR STRING; 266835.14024845; -.
DR EnsemblBacteria; BAB51447; BAB51447; BAB51447.
DR KEGG; mlo:mll4892; -.
DR PATRIC; fig|266835.9.peg.3866; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_030991_1_0_5; -.
DR OMA; QAVFHRY; -.
DR OrthoDB; 241792at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01401; PncB_like; 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 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.
FT CHAIN 1..434
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000205841"
FT MOD_RES 242
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
SQ SEQUENCE 434 AA; 49889 MW; EBA1579A9094430F CRC64;
MARTDIARRV YNHTWKLDPI VRSLLDTDFY KLLMLQMIWG MYPKVDATFS LINRTTSVRL
ADEIDEGELR EQLDHARTLR FSKKEMIWLG GNNFYGRKQI FEPEFLAWLE GFRLPDYELS
KRDGQYELSF SGPWMYTTLW EIPALAIINE LRSRAAMRAF GPFALDVLYA RAKAKMWAKT
ERLKALPGIR ISDFGTRRRH SFLWQRWCVE ALKEGIGEAF TGTSNVLLAM DNDLEALGTN
AHELPMVFAA LANSEKELKQ APYKVLQDWQ RYYGGNLLIV LPDAFGTASF LRDAPDWVAD
WTGFRPDSAP PIEGGEKILS WWRERGKDPK QKLLIFSDGL EVETIEETYR HFKGKVRMSF
GWGTNLTNDF EGCAPTETNS LDAISLVCKV TEANGRPAVK LSDNPAKATG DEKEIERYLR
IFGEKDRVEQ LVKV