ID V8IBZ8_STRMT Unreviewed; 486 AA.
AC V8IBZ8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=U758_07130 {ECO:0000313|EMBL:ETD97827.1};
OS Streptococcus mitis 27/7.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1415766 {ECO:0000313|EMBL:ETD97827.1, ECO:0000313|Proteomes:UP000018726};
RN [1] {ECO:0000313|EMBL:ETD97827.1, ECO:0000313|Proteomes:UP000018726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=27/7 {ECO:0000313|EMBL:ETD97827.1,
RC ECO:0000313|Proteomes:UP000018726};
RA Ikryannikova L.N., Ilina E.N., Kostryukova E.S., Karpova I.Y.,
RA Semashko T.A., Larin A.K., Ischenko D.S., Savinova T.A., Dubovickaya V.A.,
RA Sidorenko S.V., Govorun V.M.;
RT "Genome sequencing of Streptococcus mitis strains.";
RL Submitted (NOV-2013) 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}.
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:ETD97827.1}.
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DR EMBL; AYRS01000013; ETD97827.1; -; Genomic_DNA.
DR RefSeq; WP_023947823.1; NZ_AYRS01000013.1.
DR AlphaFoldDB; V8IBZ8; -.
DR PATRIC; fig|1415766.3.peg.1372; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000018726; 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; 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:ETD97827.1};
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 Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:ETD97827.1}.
FT DOMAIN 9..132
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 153..333
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 358..467
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 486 AA; 55113 MW; B8405C882C27031F CRC64;
MYPDDSLTLH TDLYQINMMQ VYFDQGIHNK KAVFEVYFRQ QPFKNGYAVF AGLERIVSYL
EDLRFSDSDI AYLESLGYHG AFLDYLRNFK LELTVRSAQE GDLVFANEPI VQVEGPLVQC
QLVETALLNI VNYQTLVATK AARIRSVIED EPLMEFGTRR AQEMDAAIWG TRAAVIGGAN
GTSNVRAGKL FDIPVLGTHA HALVQVYGND YEAFKAYAAT HKNCVFLVDT YDTLRIGVPA
AIQVARELGD QINFMGVRID SGDIAYISKK VRQQLDEAGF TEAKIYASND LDENTILNLK
MQKAKIDVWG VGTKLITAYD QPALGAVYKI VAIEDENGQM RNTIKLSNNA EKVSTPGKKQ
VWRITSREKG KSEGDYITYD GVDVASMTEI KMFHPTYTYI KKTVRNFDAV PLLVDIFKDG
KLIYNLPSLT EIQDYARKEF DKLWDEYKRV LNPQHYPVDL ARDVWQDKMD LIDKMRKEAL
GEGEEE
//
