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Database: UniProt
Entry: U7KD64_9CORY
LinkDB: U7KD64_9CORY
Original site: U7KD64_9CORY 
ID   U7KD64_9CORY            Unreviewed;       442 AA.
AC   U7KD64;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=HMPREF1287_01241 {ECO:0000313|EMBL:ERS44743.1};
OS   Corynebacterium sp. KPL1986.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1203619 {ECO:0000313|EMBL:ERS44743.1, ECO:0000313|Proteomes:UP000017151};
RN   [1] {ECO:0000313|EMBL:ERS44743.1, ECO:0000313|Proteomes:UP000017151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KPL1986 {ECO:0000313|EMBL:ERS44743.1,
RC   ECO:0000313|Proteomes:UP000017151};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Jacobson B., Goguen K.,
RA   Pagano E., Lemon K.P., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B., Gainer-Dewar J.,
RA   Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA   Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Corynebacterium sp. KPL1986.";
RL   Submitted (OCT-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:ERS44743.1}.
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DR   EMBL; AXLS01000002; ERS44743.1; -; Genomic_DNA.
DR   RefSeq; WP_023016972.1; NZ_KI515719.1.
DR   AlphaFoldDB; U7KD64; -.
DR   STRING; 1203619.HMPREF1287_01241; -.
DR   PATRIC; fig|1203619.3.peg.1200; -.
DR   HOGENOM; CLU_025154_3_0_11; -.
DR   OrthoDB; 9770610at2; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000017151; 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; 3.20.20.70; 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; 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:SF8; NICOTINATE PHOSPHORIBOSYLTRANSFERASE PNCB1; 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:ERS44743.1};
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:ERS44743.1}.
FT   DOMAIN          14..135
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          157..343
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
SQ   SEQUENCE   442 AA;  47889 MW;  C81E48E7E36B32E7 CRC64;
     MNDIARSIDR STALLTDKYE LTMLQAALRD GTAHRNVTCE VFSRRLPNER RYGVVAGTDR
     VLRAVEDFRF SPEQLEQMDF LDEDTRQYLR DWRFSGQIDG YREGELYFPN SPILTVRGTF
     GECVVLETIV LSILNADSAV ASAASRMVTA ADGRPILEMG SRRTHEYAAV TAARAAYLAG
     FTATSNLEAG FRYGIPVSGT AAHAWTLAHT NPDGTSNEEA AFRAQIDTLG IDTTLLVDTY
     DITKGVETAV KVGGPELGGV RIDSGDLGAV TRRVRKQLDE LGNHNTNIVV SSDLDEFAIA
     GLRGDPVDVY GVGTSVVTGS GAPTAGMVYK VVEVDGVPVA KRSSSKQSVG GAKRALRTYR
     SSGVAVEEVV YPFAAQAPDT GQLTTRELTI PLMRDGHIVE DLPDLEASRT YLNEARKTLP
     WEGLALSRDD AAVPTRMVGF KD
//
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