ID U3Q5B1_9FLAO Unreviewed; 389 AA.
AC U3Q5B1;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=K645_996 {ECO:0000313|EMBL:AGW85978.1};
OS Blattabacterium sp. (Nauphoeta cinerea).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=1316444 {ECO:0000313|EMBL:AGW85978.1, ECO:0000313|Proteomes:UP000016822};
RN [1] {ECO:0000313|EMBL:AGW85978.1, ECO:0000313|Proteomes:UP000016822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nauphoeta cinerea {ECO:0000313|Proteomes:UP000016822};
RX PubMed=24071059; DOI=10.1016/j.ygeno.2013.09.003;
RA Kambhampati S., Alleman A., Park Y.;
RT "Complete genome sequence of the endosymbiont Blattabacterium from the
RT cockroach Nauphoeta cinerea (Blattodea: Blaberidae).";
RL Genomics 102:479-483(2013).
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}.
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DR EMBL; CP005488; AGW85978.1; -; Genomic_DNA.
DR RefSeq; WP_022565028.1; NC_022550.1.
DR AlphaFoldDB; U3Q5B1; -.
DR STRING; 1316444.K645_996; -.
DR KEGG; blu:K645_996; -.
DR PATRIC; fig|1316444.3.peg.198; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_030991_1_0_10; -.
DR OrthoDB; 9771406at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000016822; 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 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:AGW85978.1};
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:AGW85978.1}.
FT DOMAIN 11..130
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 163..379
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT MOD_RES 215
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00570"
SQ SEQUENCE 389 AA; 45432 MW; 602A75934E43F0DB CRC64;
MNNSSIVSSL LDNDFYKFTM QNAVIKLFPL AKAKYEFINR GRHSFPKNFD KILEENLNKM
AYLKLSEEER IYLEKNCPYL DSSYLDFLKK YQYNPKEVNI FQKGKNIQMY IEGLWSSTIL
WEVPLMAIIS ELYYRLTGAE KISEKKIKYN KRKIKKYKKL KVRIGEYGTR RRYSYKVHKL
VLKTLIEEGL PFFMGSSNVH LSHIFSIKPI GTQGHEWIMF HAAKYGLNIA DRLAMENWLN
IYKGKLGIAL SDTYTSPIFF KNFNEKLSNL FKGVRHDSGD PIFFAKETIK HYKKFKINPI
RKKIIFSDNL DPCKVASISS FCKNKINAYF GIGTNFTNDV GLPSMNMVIK MVKALPEEKW
ISVVKLSNVK EKSTGKKNMI FLAKKILHI
//
