ID A0A348HG12_9GAMM Unreviewed; 412 AA.
AC A0A348HG12;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=ZBT109_1818 {ECO:0000313|EMBL:BBG30564.1};
OS Zymobacter palmae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Zymobacter group; Zymobacter.
OX NCBI_TaxID=33074 {ECO:0000313|EMBL:BBG30564.1, ECO:0000313|Proteomes:UP000267342};
RN [1] {ECO:0000313|EMBL:BBG30564.1, ECO:0000313|Proteomes:UP000267342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAM14233 {ECO:0000313|EMBL:BBG30564.1,
RC ECO:0000313|Proteomes:UP000267342};
RA Yanase H.;
RT "Zymobacter palmae IAM14233 (=T109) whole genome analysis.";
RL Submitted (SEP-2018) 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; AP018933; BBG30564.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A348HG12; -.
DR STRING; 1123510.GCA_000620025_01677; -.
DR KEGG; zpl:ZBT109_1818; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000267342; 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:BBG30564.1};
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:UP000267342};
KW Transferase {ECO:0000313|EMBL:BBG30564.1}.
FT DOMAIN 29..148
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 181..411
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT MOD_RES 234
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00570"
SQ SEQUENCE 412 AA; 47650 MW; 8888BEC9398F2253 CRC64;
MVKDLGDLWH GALSTTDEVT GLPMLVSILD NDFYKFTMQN AVVKLFPNAW TRYQFINRGQ
HRFPAGFADR LRHAVEGMSR LALTADERRF LEQTCPYLDP SYHDFLQGFR YDPSEVKIEQ
KGEDLEVVIE GLWYRTILWE VPIMALISEL WFQMEGQDRD SDEVSLARTH QKIEHYRQMG
IKVADFGTRR RYSYDFHDKV VSTLTEYGQE TFTGTSNVYL AYRHGIKPLG THAHEWFMFH
GAKYGFKMAN SMAMNNWVQV YRGDLGIALT DTFTTDIFFD NFDKMLAKLF DGLRHDSGDP
IVFAQKAIEH YKKMGIDPRT KTIVFSDALD PDKVDRIVEF CRDKIGMSFG IGTNFTNDVG
LKSMNMVVKM MDTRPDLSDD WLPVVKLSDI REKNTGTPEM IRLAREVLSL PN
//
