ID S9S3C8_9RALS Unreviewed; 477 AA.
AC S9S3C8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Nicotinamide phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00035036};
DE EC=2.4.2.12 {ECO:0000256|ARBA:ARBA00035024};
GN ORFNames=C404_04180 {ECO:0000313|EMBL:EPX99083.1};
OS Ralstonia sp. AU12-08.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=1235457 {ECO:0000313|EMBL:EPX99083.1, ECO:0000313|Proteomes:UP000015343};
RN [1] {ECO:0000313|EMBL:EPX99083.1, ECO:0000313|Proteomes:UP000015343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU12-08 {ECO:0000313|EMBL:EPX99083.1,
RC ECO:0000313|Proteomes:UP000015343};
RX PubMed=24503988;
RA Zhang L., Morrison M., Rickard C.M.;
RT "Draft Genome Sequence of Ralstonia pickettii AU12-08, Isolated from an
RT Intravascular Catheter in Australia.";
RL Genome Announc. 2:e00027-14(2014).
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D-
CC ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and
CC nicotinamide: step 1/1. {ECO:0000256|ARBA:ARBA00035007}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897}.
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:EPX99083.1}.
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; ASZV01000007; EPX99083.1; -; Genomic_DNA.
DR RefSeq; WP_021193325.1; NZ_ASZV01000007.1.
DR AlphaFoldDB; S9S3C8; -.
DR PATRIC; fig|1235457.3.peg.848; -.
DR eggNOG; COG1488; Bacteria.
DR Proteomes; UP000015343; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR CDD; cd01569; PBEF_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041529; DUF5598.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR016471; Nicotinamide_PRibTrfase.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR PANTHER; PTHR43816; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43816:SF1; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF18127; NAMPT_N; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR PIRSF; PIRSF005943; NMPRT; 1.
DR SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:EPX99083.1};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EPX99083.1}.
FT DOMAIN 16..107
FT /note="Nicotinamide phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18127"
FT DOMAIN 179..420
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT BINDING 187
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 210
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 236
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 299..301
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 299
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 340..341
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 371
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
FT BINDING 379
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT /evidence="ECO:0000256|PIRSR:PIRSR005943-1"
SQ SEQUENCE 477 AA; 52575 MW; F30A2CEE48014D56 CRC64;
MQNDLRRLSS ILSNPILNTD SYKASHYLQY PPGTSAMFSY IESRGGRYDS TLFFGLQMLL
KEYLSQPITT AMIDEARALF AAHGEPFNEA GWRYIVEAYG GYLPVRIRAV PEGSVVPTHN
VLVTVECDDP QVFWLTSYIE TMLLRVWYPV TVATQSWQLR QLVRRYLERT SDDISQLPFK
VHDFGARGVS SAESSAIGGA AHLVSFMGSD TVLGVVAANA YYNAPMAAFS VPAAEHSTIT
AWGRDGEGDA YRNMLRQFGK PGAIVSVVSD SYDLFAALRM WGTELRQAVI DSGATLVIRP
DSGDPQTIVM QTLRALDEAF GSMVNGKGYR VLNHVRVIQG DGVNAESIEA ILAAMEAAGY
AADNIVFGMG GALLQQLNRD TQRFAMKCSA VKVDDVWRDV CKDPVTDAGK RSKQGRLTLL
RNRQTGAYQT ATLPLAWDDR RVEGDWEEAL QTVFDGGKLL IDVSLDDVRA RAQAHEV
//
