ID A0A849MT93_UNCCR Unreviewed; 224 AA. AC A0A849MT93; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 13-SEP-2023, entry version 8. 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:NOG68629.1}; GN ORFNames=HND41_10660 {ECO:0000313|EMBL:NOG68629.1}; OS Chlorobiota bacterium. OC Bacteria; Chlorobiota. OX NCBI_TaxID=2268192 {ECO:0000313|EMBL:NOG68629.1, ECO:0000313|Proteomes:UP000591485}; RN [1] {ECO:0000313|EMBL:NOG68629.1, ECO:0000313|Proteomes:UP000591485} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHB4 {ECO:0000313|EMBL:NOG68629.1}; RA Ali M., Shaw D.R., Saikaly P.; RT "Comparative Genome-Resolved Analysis of Two Physiologically Distant RT ANAMMOX Cultures Hints Functional Redundancy in Both Ecosystems."; RL Submitted (DEC-2019) 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}. 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:NOG68629.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JABFFV010000036; NOG68629.1; -; Genomic_DNA. DR AlphaFoldDB; A0A849MT93; -. DR UniPathway; UPA00253; UER00331. DR Proteomes; UP000591485; Unassembled WGS sequence. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro. 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 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:0000313|EMBL:NOG68629.1}; KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:NOG68629.1}. FT DOMAIN 3..53 FT /note="Quinolinate phosphoribosyl transferase N-terminal" FT /evidence="ECO:0000259|Pfam:PF02749" FT DOMAIN 56..220 FT /note="Quinolinate phosphoribosyl transferase C-terminal" FT /evidence="ECO:0000259|Pfam:PF01729" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NOG68629.1" SQ SEQUENCE 224 AA; 23880 MW; C99F5FC207C5163C CRC64; ACFHKLDAQA RIRWHASDGV RIHAGQMLCE IEADTRALLS AERPALNFLQ LLSGTATVTR KYVDAVAGTR AKIVDTRKTL PGLRLAQKYA VRCGGGSNHR LGLYDGILIK ENHIMAAGGV APALAQAVKL APEGVFIQIE VESLAQLEEA LGAGAKMILL DNMDLAQMRK AVALTADRAV LEASGGVDLS KVRAIAETGV DRISIGGLTK DVRAVDLSLR HVEK //