ID W6TZ67_9SPHI Unreviewed; 373 AA.
AC W6TZ67;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU003838};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU003838};
GN ORFNames=N824_23105 {ECO:0000313|EMBL:ETZ22764.1};
OS Pedobacter sp. V48.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=509635 {ECO:0000313|EMBL:ETZ22764.1, ECO:0000313|Proteomes:UP000019145};
RN [1] {ECO:0000313|EMBL:ETZ22764.1, ECO:0000313|Proteomes:UP000019145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V48 {ECO:0000313|EMBL:ETZ22764.1,
RC ECO:0000313|Proteomes:UP000019145};
RX PubMed=24578271;
RA Bitzer A.S., Garbeva P., Silby M.W.;
RT "Draft Genome Sequence of Pedobacter sp. Strain V48, Isolated from a
RT Coastal Sand Dune in the Netherlands.";
RL Genome Announc. 2:e00094-e00014(2014).
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|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;
CC Evidence={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|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|RuleBase:RU003838}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, 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:ETZ22764.1}.
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DR EMBL; AWRU01000009; ETZ22764.1; -; Genomic_DNA.
DR AlphaFoldDB; W6TZ67; -.
DR STRING; 509635.N824_23105; -.
DR PATRIC; fig|509635.5.peg.2368; -.
DR eggNOG; COG1488; Bacteria.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000019145; 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 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:ETZ22764.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU003838};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU003838}; Transferase {ECO:0000313|EMBL:ETZ22764.1}.
FT DOMAIN 1..110
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 146..370
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
SQ SEQUENCE 373 AA; 42770 MW; CC02D359216E7B97 CRC64;
MQQGVIRLFP AAKARYAFIN RGKHSFPDGF AKALREAVNE MATLKLSREE KHFLQVNCPY
LDPVYLDFLE GYRYNPEEIY ITQNGDQLEV HVEGLWYRTI LWEVPLMSLI CELFYILNDS
QRISNDEVIN HTKEKIENYR RLGVTVAEFG TRRRYSYQVH RLVLQALSQY GEGSFIGTSN
VHMAMIHKTK PIGTHAHEWF MFHAARYGFK MANATGLEHW VAVYRGDLGI ALSDTYTTEV
FFKQFDKMFS KLFDGVRHDS GDALLFADKV ISHYNSMGID PRTKTIIFSD GLNYEKVARI
ADHCRDKIGM SFGIGTNLTN DAGPEAMNIV IKMTEAQPKD GEWTEVVKLS DEPGKHTGTE
RMINLAKTIL EID
//
