ID S3V6K9_9LEPT Unreviewed; 303 AA.
AC S3V6K9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
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:EPG67937.1};
GN ORFNames=LEP1GSC061_0659 {ECO:0000313|EMBL:EPG67937.1};
OS Leptospira wolffii serovar Khorat str. Khorat-H2.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1193069 {ECO:0000313|EMBL:EPG67937.1, ECO:0000313|Proteomes:UP000014564};
RN [1] {ECO:0000313|EMBL:EPG67937.1, ECO:0000313|Proteomes:UP000014564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Khorat-H2 {ECO:0000313|EMBL:EPG67937.1,
RC ECO:0000313|Proteomes:UP000014564};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (APR-2013) 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:EPG67937.1}.
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DR EMBL; AKWX02000004; EPG67937.1; -; Genomic_DNA.
DR RefSeq; WP_016543839.1; NZ_AKWX02000004.1.
DR AlphaFoldDB; S3V6K9; -.
DR STRING; 1193069.LEP1GSC061_0659; -.
DR UniPathway; UPA00253; UER00331.
DR Proteomes; UP000014564; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR006250}.
FT DOMAIN 41..129
FT /note="Quinolinate phosphoribosyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02749"
FT DOMAIN 131..298
FT /note="Quinolinate phosphoribosyl transferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01729"
SQ SEQUENCE 303 AA; 33797 MW; A177362E357EB330 CRC64;
MRKTFRNGET KVKRAYTKPI SQLTEEDYFP LAKMAWDEDC PDQDITSVSL FPPDKKAVAN
LNAREEGVLC GRGVSEVLAK LSGGDLKFDF RFSDGDRFHA GDTIAIIQGS LLSLLRVERI
LLNFLQYLSG ISSTTRKVVD QYGSKGIMIL DTRKTLPGYR KLAKYAVYCG GGSNHRLDLS
EMAMIKDNHL AMFESAKIPV GKIRDGFPGR LVELEIDSLE QLEDALNAEP DVLMLDNFSI
PDTRTAYKRS KEKNRNILIE CSGGITPEKL EALSEFPGVG VSMGYLTHTT RFLDLGLDIR
TDN
//
