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Database: UniProt
Entry: R5U026_9BACE
LinkDB: R5U026_9BACE
Original site: R5U026_9BACE 
ID   R5U026_9BACE            Unreviewed;       284 AA.
AC   R5U026;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=BN759_00806 {ECO:0000313|EMBL:CCZ71395.1};
OS   Bacteroides sp. CAG:702.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1262747 {ECO:0000313|EMBL:CCZ71395.1, ECO:0000313|Proteomes:UP000017962};
RN   [1] {ECO:0000313|EMBL:CCZ71395.1, ECO:0000313|Proteomes:UP000017962}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:702 {ECO:0000313|Proteomes:UP000017962};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ71395.1}.
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DR   EMBL; CBAM010000233; CCZ71395.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5U026; -.
DR   STRING; 1262747.BN759_00806; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000017962; 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   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|PIRNR:PIRNR006250};
KW   Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017962};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          22..111
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          113..282
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         134..136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         158
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         246..248
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
FT   BINDING         267..269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006250-1"
SQ   SEQUENCE   284 AA;  31493 MW;  19583A9211DEE9ED CRC64;
     MDEKIVKDLI DRLIDLSFAE DIGDGDHTTL SCIPADAMGK SKLLIKEEGI LAGIEVAKEV
     FRRFDPTLKV EVFILDGAHV KPGDVPMIVS GKVQSLLQTE RLMLNIMQRM SGIATMTHKY
     VERLEGTKTR VLDTRKTTPG MRILEKMAVK IGGGVNHRIG LFDMILLKDN HVDFAGGIDK
     AILRAKEYCK EKGKDLKIEI EVRNFDELQQ VLDLGGVDRI MLDNFTPADT RKAVEMVGGR
     YEIESSGGIT FDTLRDYAEC GVDFISVGAL THSVKGLDMS FKAC
//
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