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Database: UniProt
Entry: A0A1T5IK99_9MICO
LinkDB: A0A1T5IK99_9MICO
Original site: A0A1T5IK99_9MICO 
ID   A0A1T5IK99_9MICO        Unreviewed;       334 AA.
AC   A0A1T5IK99;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN04324258_0632 {ECO:0000313|EMBL:SKC39567.1};
OS   Krasilnikoviella flava.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Krasilnikoviella.
OX   NCBI_TaxID=526729 {ECO:0000313|EMBL:SKC39567.1, ECO:0000313|Proteomes:UP000189777};
RN   [1] {ECO:0000313|EMBL:SKC39567.1, ECO:0000313|Proteomes:UP000189777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21481 {ECO:0000313|EMBL:SKC39567.1,
RC   ECO:0000313|Proteomes:UP000189777};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; FUZQ01000001; SKC39567.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T5IK99; -.
DR   STRING; 526729.SAMN04324258_0632; -.
DR   UniPathway; UPA00253; UER00331.
DR   Proteomes; UP000189777; 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:UP000189777};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT   DOMAIN          61..154
FT                   /note="Quinolinate phosphoribosyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02749"
FT   DOMAIN          156..329
FT                   /note="Quinolinate phosphoribosyl transferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01729"
SQ   SEQUENCE   334 AA;  34274 MW;  811AA302272B9D2F CRC64;
     MRRQGPAARA VALRSVTATH RDLPQDLPVH DQPSAVEPGL DAAWVARTVE TALDEDLGTA
     PGRDVTTQAT VPTTATGTAD LVARSAGTVA GLVVVAETLR QVAGRLGLPA PVVTFHAQDG
     DAVAPGQVLA ALAGPVQVLL VAERTLLNLA SRASGVATAT AAWSRELAGT GAQVLDTRKT
     TPGLRALEKY AVRAGGGTNK RMGLHDVAMV KDNHVVAAGS VRGAIDAVRR TFPDVLVQVE
     ADTTDQASEA LDAGADFLLL DNMPTPVLAA TVAAVRARQG RDGAPVHVEL EATGNLTLDR
     AREVAATGVD YLSVGALTHS APILDLALDL RPGS
//
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