ID A0A2N4UFP9_9BURK Unreviewed; 391 AA.
AC A0A2N4UFP9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 ECO:0000313|EMBL:PLC53848.1};
GN ORFNames=CR155_10415 {ECO:0000313|EMBL:PLC53848.1};
OS Pollutimonas nitritireducens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pollutimonas.
OX NCBI_TaxID=2045209 {ECO:0000313|EMBL:PLC53848.1, ECO:0000313|Proteomes:UP000234328};
RN [1] {ECO:0000313|EMBL:PLC53848.1, ECO:0000313|Proteomes:UP000234328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JR1/69-2-13 {ECO:0000313|EMBL:PLC53848.1,
RC ECO:0000313|Proteomes:UP000234328};
RA Grouzdev D.S., Tourova T.P., Goeva M.A., Babich T.L., Sokolova D.S.,
RA Abdullin R., Poltaraus A.B., Toshchakov S.V., Nazina T.N.;
RT "Two draft genome sequences of Pusillimonas sp. strains isolated from a
RT nitrate- and radionuclide-contaminated groundwater in Russia.";
RL Submitted (OCT-2017) 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:PLC53848.1}.
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DR EMBL; PDNV01000006; PLC53848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N4UFP9; -.
DR OrthoDB; 9771406at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000234328; 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; cd01401; PncB_like; 1.
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:PLC53848.1};
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:UP000234328};
KW Transferase {ECO:0000313|EMBL:PLC53848.1}.
FT DOMAIN 7..127
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 163..389
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT MOD_RES 216
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00570"
SQ SEQUENCE 391 AA; 44700 MW; 6AFE141575875D97 CRC64;
MIITSLLDTD LYKFTMMQVV LHHFPAAQVE YRYKCRTPNV NLQPYLDEIR SEIHALCQLQ
FTEEELHYLR SLRFLKSDFV DFLGLFHMPE KCITVSAGAV KGEIDISVKG PWLHTILFEI
PVLAIVNEVY FRNVCREPAW EEGRKRLQSK MQLVSDDPAL ADFRVAEYGT RRRFSKKWHE
EVVLTMKSQM SPHFAGTSNV RLAMKHGVTP LGTMGHEYLQ ACQALGPRLR DSQVFALEVW
AKEYRGDLGI ALSDVYGMDA FLRDFDMYFC KLFDGARHDS GDPFIWGERL LAHYAANRAD
PRTKTLVFSD ALTIPRAIEL AKHFAGRCKI SFGIGTNLTN DLGHEPLQIV MKMVRCNGQP
VAKVSDAPEK TMCDDPAYLA YLRQVFQLPP P
//