ID E6YXM3_BARSR Unreviewed; 434 AA.
AC E6YXM3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
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:CBI81611.1};
GN ORFNames=B11C_10085 {ECO:0000313|EMBL:CBI81611.1}, BscR1v2_000850
GN {ECO:0000313|EMBL:AQX30042.1};
OS Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=687861 {ECO:0000313|EMBL:CBI81611.1};
RN [1] {ECO:0000313|EMBL:CBI81611.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R1 {ECO:0000313|EMBL:CBI81611.1};
RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT "Parallel evolution of a type IV secretion system in radiating lineages of
RT the host-restricted bacterial pathogen Bartonella.";
RL PLoS Genet. 7:E1001296-E1001296(2011).
RN [2] {ECO:0000313|Proteomes:UP000190811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 {ECO:0000313|Proteomes:UP000190811};
RX PubMed=28338931; DOI=10.1093/gbe/evx042;
RA Harms A., Segers F.H., Quebatte M., Mistl C., Manfredi P., Korner J.,
RA Chomel B.B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT "Evolutionary Dynamics of Pathoadaptation Revealed by Three Independent
RT Acquisitions of the VirB/D4 Type IV Secretion System in Bartonella.";
RL Genome Biol. Evol. 9:761-776(2017).
RN [3] {ECO:0000313|EMBL:AQX30042.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R1 {ECO:0000313|EMBL:AQX30042.1};
RA Harms A., Segers F.H.I.D., Quebatte M., Mistl C., Manfredi P., Koerner J.,
RA Chomel B., Kosoy M., Maruyama S., Engel P., Dehio C.;
RT "Evolutionary dynamics of pathoadaptation revealed by three independent
RT acquisitions of the VirB/D4 type IV secretion system in Bartonella.";
RL Submitted (FEB-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}.
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DR EMBL; CP019789; AQX30042.1; -; Genomic_DNA.
DR EMBL; FN645506; CBI81611.1; -; Genomic_DNA.
DR AlphaFoldDB; E6YXM3; -.
DR STRING; 687861.BscR1v2_000850; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000190811; Chromosome.
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:CBI81611.1};
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 Transferase {ECO:0000313|EMBL:CBI81611.1}.
FT DOMAIN 25..149
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 190..418
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT MOD_RES 242
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00570"
SQ SEQUENCE 434 AA; 50009 MW; 0784B655AF3EB41D CRC64;
MNHTDIARRV YNHTWKLDPI IRSLLDTDFY KLLMVQMIWG LYPNVHVTFS LINRSKTICL
ANDIDEDELR AQLDHALSLR FTKKEIIWLA GNTFYGRKQI FKPDFLNWLE KFQLPEYELT
QKDGQYILRF HGPWAYSSMW EIPALSIISE LRSRAAIKNL GRFALDVLYA RAKAKMWSKI
ERLKQLPDLN IADFGTRRRH SFLWQRWCVE ALKEGIGNSL VGSSNILLAM DTDLEALGTN
AHELPMVIAA LANNDNDLHQ ASYQVLQNWN RYYGGNLLIV LPDAFGTEAF LRNAPDWVAD
WTGFRIDSAL PIEGGERIIK WWQEKGKNPQ EKLLIFSDAL DVDTIEKTYH HFHGKVRMSF
GWGTNLTNDF ENCAPQNIAN LEAASLVCKA THANGRPTVK LSDNPEKAIG DPQEIQRYLN
FFNPELSTTK PIKI
//
