ID A0A0B4EJM7_9RHOB Unreviewed; 429 AA.
AC A0A0B4EJM7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=GC1_12635 {ECO:0000313|EMBL:KID08887.1};
OS Leisingera sp. ANG1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1002340 {ECO:0000313|EMBL:KID08887.1, ECO:0000313|Proteomes:UP000031201};
RN [1] {ECO:0000313|EMBL:KID08887.1, ECO:0000313|Proteomes:UP000031201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG1 {ECO:0000313|EMBL:KID08887.1,
RC ECO:0000313|Proteomes:UP000031201};
RX PubMed=21551313; DOI=10.1128/JB.05139-11;
RA Collins A.J., Nyholm S.V.;
RT "Draft genome of Phaeobacter gallaeciensis ANG1, a dominant member of the
RT accessory nidamental gland of Euprymna scolopes.";
RL J. Bacteriol. 193:3397-3398(2011).
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:KID08887.1}.
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DR EMBL; AFCF02000007; KID08887.1; -; Genomic_DNA.
DR RefSeq; WP_019295050.1; NZ_AFCF02000007.1.
DR AlphaFoldDB; A0A0B4EJM7; -.
DR STRING; 1002340.GC1_12635; -.
DR eggNOG; COG1488; Bacteria.
DR OrthoDB; 9771406at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000031201; 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 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:KID08887.1};
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:KID08887.1}.
FT DOMAIN 22..145
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 187..420
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT MOD_RES 239
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00570"
SQ SEQUENCE 429 AA; 49083 MW; 578F03364E0F7436 CRC64;
MDIATRVYNH KWKIDPIVRS LIDTDFYKLL MCQSVFRNKP DTTVTFSLIN RSAQVPLAKL
IDEGELREQL DHIRSLSLSR GESTWLRGNT FYGKRQMFRP DFMEWFEGLR LPPYHLERKG
DQYELTFEGK WHEVMLWEIP ALAVLMELRS RAVINSMGRF ELQVLYARAM TRVWEKIERL
REVEGLTIAD FGTRRRHSFL WQDWCVQAMI EGLGEKFTGT SNCLIAMRRE VEAIGTNAHE
LPMVYSALAG SDAELAQAPY DVLSDWHDEH EGNLRIILPD TYGTQGFLDR APDWLAGWTG
IRIDSGDPAK GAEVAINWWK ARGEDPAEKR VIFSDGLDVQ QIQDLHAQFS GRTKVSFGWG
TLLTNDFRKL VPDDALAPFS LVCKAVAANG RPTVKLSDNP EKAMGPADEI TRYKRVFGVG
EQERQAVIV
//