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Database: UniProt
Entry: A0A0N1MGA0_9FLAO
LinkDB: A0A0N1MGA0_9FLAO
Original site: A0A0N1MGA0_9FLAO 
ID   A0A0N1MGA0_9FLAO        Unreviewed;       286 AA.
AC   A0A0N1MGA0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=nicotinate-nucleotide diphosphorylase (carboxylating) {ECO:0000256|ARBA:ARBA00011944};
DE            EC=2.4.2.19 {ECO:0000256|ARBA:ARBA00011944};
DE   AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating] {ECO:0000256|ARBA:ARBA00033102};
GN   ORFNames=AMQ68_19125 {ECO:0000313|EMBL:KPH11514.1};
OS   Chryseobacterium sp. ERMR1:04.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1705393 {ECO:0000313|EMBL:KPH11514.1, ECO:0000313|Proteomes:UP000037945};
RN   [1] {ECO:0000313|EMBL:KPH11514.1, ECO:0000313|Proteomes:UP000037945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERMR1:04 {ECO:0000313|EMBL:KPH11514.1,
RC   ECO:0000313|Proteomes:UP000037945};
RX   PubMed=26543128;
RA   Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT   "Genome Assembly of Chryseobacterium polytrichastri ERMR1:04, a
RT   Psychrotolerant Bacterium with Cold Active Proteases, Isolated from East
RT   Rathong Glacier in India.";
RL   Genome Announc. 3:e01305-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000037945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERMR1:04 {ECO:0000313|Proteomes:UP000037945};
RA   Swarnkar M.K., Kumar R., Singh A.K., Singh D.;
RT   "Genome Sequencing of Chryseobacterium sp. ERMR1:04 isolated from Glacier
RT   Moraine Ridge soil.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA).
CC       {ECO:0000256|ARBA:ARBA00003237}.
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC       ribonucleotide from quinolinate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004893}.
CC   -!- SIMILARITY: Belongs to the NadC/ModD family.
CC       {ECO:0000256|ARBA:ARBA00009400, ECO:0000256|PIRNR:PIRNR006250}.
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:KPH11514.1}.
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DR   EMBL; LIRF01000008; KPH11514.1; -; Genomic_DNA.
DR   RefSeq; WP_054512197.1; NZ_LIRF01000008.1.
DR   AlphaFoldDB; A0A0N1MGA0; -.
DR   STRING; 1705393.AMQ68_19125; -.
DR   PATRIC; fig|1705393.3.peg.4026; -.
DR   OrthoDB; 9782546at2; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000037945; Unassembled WGS sequence.
DR   GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01572; QPRTase; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.90.1170.20; Quinolinate phosphoribosyl transferase, N-terminal domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR004393; NadC.
DR   InterPro; IPR027277; NadC/ModD.
DR   InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR   InterPro; IPR037128; Quinolinate_PRibosylTase_N_sf.
DR   InterPro; IPR002638; Quinolinate_PRibosylTrfase_C.
DR   InterPro; IPR022412; Quinolinate_PRibosylTrfase_N.
DR   NCBIfam; TIGR00078; nadC; 1.
DR   PANTHER; PTHR32179; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE [CARBOXYLATING]; 1.
DR   PANTHER; PTHR32179:SF3; NICOTINATE-NUCLEOTIDE PYROPHOSPHORYLASE [CARBOXYLATING]; 1.
DR   Pfam; PF01729; QRPTase_C; 1.
DR   Pfam; PF02749; QRPTase_N; 1.
DR   PIRSF; PIRSF006250; NadC_ModD; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|PIRNR:PIRNR006250};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          25..113
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          115..283
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
FT   COILED          193..220
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         136..138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         247..249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         268..270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ   SEQUENCE   286 AA;  31901 MW;  90350858BBF4497A CRC64;
     MKRPDYVTDK VLKQFIKNAL EEDIQDGDHS TLSTIPKDLE QSAKLLVKQN CILAGVELAE
     IIFKTFDKNL KVEVFIKDGT PARIGDVALI VTGSARSILS TERLILNCMQ RMSGIATLTN
     DWDSRLVGTK TKLLDTRKTT PNFRVCEKWA VAIGGGTNHR YGLYDMIMLK DNHIDYNGSI
     TNAVKMAKDY IKKNKKKLKI EVETRNLEEV EEAIKAKVDR IMLDNMNVKM MKQAVKMING
     SCESEASGGI TRDMLKEIAT TGVTYISVGA LTHSAENIDL SLKAVK
//
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