ID F5L6D7_CALTT Unreviewed; 480 AA.
AC F5L6D7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN ORFNames=CathTA2_1349 {ECO:0000313|EMBL:EGL83090.1}, HUR95_10405
GN {ECO:0000313|EMBL:QZT32790.1};
OS Caldalkalibacillus thermarum (strain TA2.A1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Caldalkalibacillus.
OX NCBI_TaxID=986075 {ECO:0000313|EMBL:EGL83090.1, ECO:0000313|Proteomes:UP000010716};
RN [1] {ECO:0000313|EMBL:EGL83090.1, ECO:0000313|Proteomes:UP000010716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:EGL83090.1,
RC ECO:0000313|Proteomes:UP000010716};
RX PubMed=21685297; DOI=10.1128/JB.05035-11;
RA Kalamorz F., Keis S., McMillan D.G., Olsson K., Stanton J.A., Stockwell P.,
RA Black M.A., Klingeman D.M., Land M.L., Han C.S., Martin S.L., Becher S.A.,
RA Peddie C.J., Morgan H.W., Matthies D., Preiss L., Meier T., Brown S.D.,
RA Cook G.M.;
RT "Draft genome sequence of the thermoalkaliphilic Caldalkalibacillus
RT thermarum strain TA2.A1.";
RL J. Bacteriol. 193:4290-4291(2011).
RN [2] {ECO:0000313|EMBL:QZT32790.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT32790.1};
RX PubMed=33030592;
RA de Jong S.I., van den Broek M.A., Merkel A.Y., de la Torre Cortes P.,
RA Kalamorz F., Cook G.M., van Loosdrecht M.C.M., McMillan D.G.G.;
RT "Genomic analysis of Caldalkalibacillus thermarum TA2.A1 reveals aerobic
RT alkaliphilic metabolism and evolutionary hallmarks linking alkaliphilic
RT bacteria and plant life.";
RL Extremophiles 24:923-935(2020).
RN [3] {ECO:0000313|EMBL:QZT32790.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TA2.A1 {ECO:0000313|EMBL:QZT32790.1};
RA de Jong S., van den Broek M., Merkel A., de la Torre Cortes P.,
RA Kalamorz F., Cook G., van Loosdrecht M., McMillan D.;
RL Submitted (AUG-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC {ECO:0000256|RuleBase:RU365100}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001240,
CC ECO:0000256|RuleBase:RU365100};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
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|RuleBase:RU365100}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
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DR EMBL; AFCE01000125; EGL83090.1; -; Genomic_DNA.
DR EMBL; CP082237; QZT32790.1; -; Genomic_DNA.
DR AlphaFoldDB; F5L6D7; -.
DR KEGG; cthu:HUR95_10405; -.
DR eggNOG; COG1488; Bacteria.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000010716; Unassembled WGS sequence.
DR Proteomes; UP000825179; 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 CDD; cd01570; NAPRTase_A; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR041619; NAPRTase_C.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR NCBIfam; TIGR01513; NAPRTase_put; 1.
DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17956; NAPRTase_C; 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:EGL83090.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365100};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU365100};
KW Reference proteome {ECO:0000313|Proteomes:UP000010716};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:EGL83090.1}.
FT DOMAIN 5..129
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 150..320
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 360..468
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 480 AA; 54279 MW; 5D081AEA3201747E CRC64;
MNKTLLTDLY QINMMYAHYK NGKLNQQTVF DLYYRTNPGQ SGYAIMAGLE QVVEYICQLS
FTEEDIAYLR SVERYDENFI DYLKQFRFTG EIYAVPEGTV VFPHEPLLRV KAPIGEAQLI
ETAVLNIINH QTLIATKASR ITEAAGGGLV MEFGLRRAQG PDAGVYGARA AFIGGVQATS
NVLAGKKFGI PVKGTHSHAY VQSYPSEYEA FLAFARTFPH NCILLVDTYD TLNSGVPNAI
KTFKKMKEEL GDKFKNYGIR LDSGDLAYLS KAARKMLDEA GFEDAIIVAS SDLDEYLIRD
LRAQGAQIDA WGVGTNLITS RDCPALGGVY KLVAEEENGR LVPKIKVSEN PQKITNPGYK
KVVRFYDRNS KQALVDLIML EEEPIPTESF IAFDPVNTWK RKTVENFEAR ELLAPIFKNG
ELVCELPDLT EIQRYAQREK ERFAPEIRRL INPHVYHVDL SHQLWELKHR LLSQAKQLRT
//
