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Database: UniProt
Entry: C6YWC5_9GAMM
LinkDB: C6YWC5_9GAMM
Original site: C6YWC5_9GAMM 
ID   C6YWC5_9GAMM            Unreviewed;       287 AA.
AC   C6YWC5;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 59.
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   Name=nadC {ECO:0000313|EMBL:AJI75650.1};
GN   ORFNames=BZ13_154 {ECO:0000313|EMBL:AJI75650.1};
OS   Francisella philomiragia subsp. philomiragia ATCC 25015.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=539329 {ECO:0000313|EMBL:AJI75650.1, ECO:0000313|Proteomes:UP000031897};
RN   [1] {ECO:0000313|EMBL:AJI75650.1, ECO:0000313|Proteomes:UP000031897}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O#319L {ECO:0000313|EMBL:AJI75650.1,
RC   ECO:0000313|Proteomes:UP000031897};
RX   PubMed=25931589;
RA   Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G.,
RA   Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Chertkov O.,
RA   Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., Gibbons H.S.,
RA   Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.;
RT   "Genome sequencing of 18 francisella strains to aid in assay development
RT   and testing.";
RL   Genome Announc. 3:0-0(2015).
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}.
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DR   EMBL; CP010019; AJI75650.1; -; Genomic_DNA.
DR   RefSeq; WP_004287846.1; NZ_DS999316.1.
DR   AlphaFoldDB; C6YWC5; -.
DR   KEGG; fpt:BZ13_154; -.
DR   PATRIC; fig|539329.6.peg.155; -.
DR   HOGENOM; CLU_039622_0_3_6; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000031897; Chromosome.
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   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          33..118
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          121..284
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         141..143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         165
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         248..250
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         269..271
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ   SEQUENCE   287 AA;  31504 MW;  7C7E0C02877A5B48 CRC64;
     MSEIMLNTNQ ITSVPENVIK KLVAESLVED IADGDITAQL AEDVDTTAFC ITREDMVLCG
     KEFANEVINQ VDKNIQIIWF YDDADKISAD EKIFELRGNA RSILTAERAM LNFIQMLSAT
     ATATNNLVKL IADYKTKLLD TRKTIPCFRM AQKYAVTCGG GFNHRIGLFD AYLIKENHIR
     SAGGIAKAVS KAARLQPTKT IEVEVTNLDE LNQAIQAGAN IIMLDNFSIE DINKAVEIAK
     DKVALEVSGN IDSNSIVKMA QTGVDFISVG AITKHITAID LSMQVQL
//
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