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Database: UniProt
Entry: M5AM87_RHILI
LinkDB: M5AM87_RHILI
Original site: M5AM87_RHILI 
ID   M5AM87_RHILI            Unreviewed;       293 AA.
AC   M5AM87;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
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:BAN09605.1};
OS   Rhizobium loti (Mesorhizobium loti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=381 {ECO:0000313|EMBL:BAN09605.1};
RN   [1] {ECO:0000313|EMBL:BAN09605.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NZP2037 {ECO:0000313|EMBL:BAN09605.1};
RA   Maita H., Sato S.;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAN09605.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NZP2037 {ECO:0000313|EMBL:BAN09605.1};
RX   PubMed=23666538;
RA   Kasai-Maita H., Hirakawa H., Nakamura Y., Kaneko T., Miki K., Maruya J.,
RA   Okazaki S., Tabata S., Saeki K., Sato S.;
RT   "Commonalities and Differences among Symbiosis Islands of Three
RT   Mesorhizobium loti Strains.";
RL   Microbes Environ. 28:275-278(2013).
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; AP012557; BAN09605.1; -; Genomic_DNA.
DR   RefSeq; WP_019863264.1; NZ_LZTL01000004.1.
DR   OrthoDB; 9782546at2; -.
DR   UniPathway; UPA00253; UER00331.
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          26..114
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          116..281
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   293 AA;  30626 MW;  D08F8B49F49A7A0F CRC64;
     MTSLAPLPQI IMEPIVRNAL LEDLGRAGDI TSDAIIPADC KATLSLNARQ AGVVAGLDLV
     MFAFLLVDPG ISIQLRCPEG GKISTGQTIA IVNGPARSLL TAERTALNFL CKLSGIATAT
     ATLVNAVRGH NAKIVCTRKT TPGLRVLEKY AVRAGGGANH RFALDDAVLI KDNHIAIAGD
     IRTAIERARS AIGHMVKIEV EVDRLDQLEI ALAAGVDAVL LDNMSVEDLA QAVAMVGGRA
     ITEASGRVTR ASAAAIAATG VDLISVGWLT HSAPILDIGL DMPADRNCNR HLN
//
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