ID A0A2U3C036_9ACTN Unreviewed; 344 AA.
AC A0A2U3C036;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=CK485_08600 {ECO:0000313|EMBL:PWI42415.1};
OS Streptomyces sp. ICBB 8177.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=563922 {ECO:0000313|EMBL:PWI42415.1, ECO:0000313|Proteomes:UP000245673};
RN [1] {ECO:0000313|EMBL:PWI42415.1, ECO:0000313|Proteomes:UP000245673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICBB 8177 {ECO:0000313|EMBL:PWI42415.1,
RC ECO:0000313|Proteomes:UP000245673};
RX PubMed=29773836; DOI=10.1038/s41598-018-26179-w;
RA Pavlikova M., Kamenik Z., Janata J., Kadlcik S., Kuzma M., Najmanova L.;
RT "Novel pathway of 3-hydroxyanthranilic acid formation in limazepine
RT biosynthesis reveals evolutionary relation between phenazines and
RT pyrrolobenzodiazepines.";
RL Sci. Rep. 8:7810-7810(2018).
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}.
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:PWI42415.1}.
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DR EMBL; NSKH01000018; PWI42415.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U3C036; -.
DR OrthoDB; 9782546at2; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000245673; 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 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:0000256|ARBA:ARBA00022676};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW Reference proteome {ECO:0000313|Proteomes:UP000245673};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 77..164
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 166..330
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
SQ SEQUENCE 344 AA; 35998 MW; 52B1019BFCCCC575 CRC64;
MSTPDLPLIQ IGRPGEGAGG GCGDGCGCGG DDAYALDPLE CGLDPDLAQL LADAGLDPVQ
VEDIAHMAIE EDLDNGVDVT TVATIPEDAV AVGDFTARQA GVVAGLRIAE AVLSVVCTDE
FEVERHVEDG DRVEPGQVLL SVRTRTRDLL TAERSALNLL CRLSGIATAT RAWADVLEGT
RTRVRDTRKT TPGLRALEKY AVRCGGGVNH RMSLSDAALV KDNHVVAAGG VAQAFRAVRE
EFPDLAIEVE VDTLHQVREV LDAGADLILL DNFTPAETEE AVAIVAGRAA LESSGRLTLD
VARAYAAAGV DYLAVGALTH SSPVLDIGLD LREQAADDTA DAED
//