ID A0A2S8SSU5_9BACT Unreviewed; 514 AA.
AC A0A2S8SSU5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=B1R32_10890 {ECO:0000313|EMBL:PQV63883.1};
OS Abditibacterium utsteinense.
OC Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales;
OC Abditibacteriaceae; Abditibacterium.
OX NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV63883.1, ECO:0000313|Proteomes:UP000237684};
RN [1] {ECO:0000313|EMBL:PQV63883.1, ECO:0000313|Proteomes:UP000237684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV63883.1,
RC ECO:0000313|Proteomes:UP000237684};
RX PubMed=29475572;
RA Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL Syst. Appl. Microbiol. 0:0-0(2018).
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:PQV63883.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NIGF01000008; PQV63883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8SSU5; -.
DR InParanoid; A0A2S8SSU5; -.
DR OrthoDB; 9770610at2; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000237684; 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:PQV63883.1};
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:UP000237684};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:PQV63883.1}.
FT DOMAIN 12..142
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 164..345
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT DOMAIN 388..480
FT /note="Nicotinate phosphoribosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17956"
SQ SEQUENCE 514 AA; 56243 MW; DDD4B5F42FFCAD6D CRC64;
MQNLFFPGSS ALLTDLYQLT MAYGYWKSGR AETLANFQLY FRKQPFNGGF SVACGLAPAL
EWIENFGFDA SDLEYLGTLT GADDKALFEL KFLEYLGDLK LEIDIDAMPE GTICFAQEPL
VRVQGPILQC QLLETALLNI INFQTLIATK AARIVLAARG EPILEFGARR AQNIDGALSA
SRAAFVGGVA ATSNVLAGKL FGIPVKGTHA HSWVMLFDSE LEAFETYADA LPNNVVFLVD
TYDTLEGVRH ACEVGHKLRQ KGHDLLGVRL DSGDLAYLSI EARKILDENG FPEAKIYASN
DLDEHLISSL KEQGAQIAVW GVGTRLVTGH DQPALGGVYK LTAIRDDKTQ AWQPRVKLSE
QSVKISTPGV VGARRYFSGE GDKCQNVADA IYEVGAQPRG GLVIVDPLDS LHRRRIAANL
SSRELLEPVV RGGNRVGEMP QLADSRDRTL RELEHFVAGV KRFVNPHVYP VGLEASLHEK
KMDLVLRARG VTAGKDVENE AETADLELTS KLDA
//
