ID A0A1M9KKR0_9MYCO Unreviewed; 434 AA.
AC A0A1M9KKR0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU365100};
GN Name=pncB {ECO:0000313|EMBL:SKQ52699.1};
GN ORFNames=SAMEA2070793_02754 {ECO:0000313|EMBL:SHY86515.1},
GN SAMEA2071181_00878 {ECO:0000313|EMBL:SKQ52699.1};
OS Mycobacteroides abscessus subsp. abscessus.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=1185650 {ECO:0000313|EMBL:SKQ52699.1, ECO:0000313|Proteomes:UP000190796};
RN [1] {ECO:0000313|Proteomes:UP000184807, ECO:0000313|Proteomes:UP000190796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22 {ECO:0000313|EMBL:SKQ52699.1,
RC ECO:0000313|Proteomes:UP000190796}, and 425
RC {ECO:0000313|EMBL:SHY86515.1, ECO:0000313|Proteomes:UP000184807};
RG Pathogen Informatics;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate.
CC {ECO:0000256|RuleBase:RU365100}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide +
CC phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:456216; EC=6.3.4.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001240,
CC ECO:0000256|RuleBase:RU365100};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU365100}.
CC -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC cycle. Phosphorylation strongly increases the affinity for substrates
CC and increases the rate of nicotinate D-ribonucleotide production.
CC Dephosphorylation regenerates the low-affinity form of the enzyme,
CC leading to product release. {ECO:0000256|RuleBase:RU365100}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU365100}.
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:SKQ52699.1}.
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DR EMBL; FSFZ01000002; SHY86515.1; -; Genomic_DNA.
DR EMBL; FVKR01000002; SKQ52699.1; -; Genomic_DNA.
DR RefSeq; WP_005093052.1; NZ_SAZC01000014.1.
DR AlphaFoldDB; A0A1M9KKR0; -.
DR GeneID; 66971858; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000184807; Unassembled WGS sequence.
DR Proteomes; UP000190796; Unassembled WGS sequence.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01570; NAPRTase_A; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR NCBIfam; TIGR01513; NAPRTase_put; 1.
DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11098:SF8; NICOTINATE PHOSPHORIBOSYLTRANSFERASE PNCB1; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 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:0000313|EMBL:SKQ52699.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365100};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU365100};
KW Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:SKQ52699.1}.
FT DOMAIN 8..130
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 152..340
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
SQ SEQUENCE 434 AA; 45915 MW; 3ECD2BE51F587849 CRC64;
MTHPCTSLLT DKYELTMLAA ALRDGTAGRR ATFEVFARRL PDGRRYGVVA GTGRLLEALA
EFRFGPAELE SVSTFLDEDS LEYLAAYRFG GDIDGYPEGE LYFPGSPVLT LRGSFAECVI
LETLILSILN HDSAVASAAA RMVSAAGDRP LIEMGSRRTH ELAAVACARA AYLAGFESTS
NLEAQRRYGV PARGTAAHAF TLLHAKDGMS PGEAEREAFR AQVEALGVGT TLLVDTYDIT
AGVENAIAVA GTALGAVRID SGDLGMLARQ VRAQLDALGA HRTRIVVSGD LDEYSIAALR
AEPVDIYGVG TSVVTGSGIP TAGMVYKLVE IDGIPVAKRS SHKESHGGHK CALRIAKPTG
TITEEVVYRA DAGQPTVPEP HRILTTALVR GGKPVAYHSL TEARNRVHAG LLSLPWEGLG
LSHGDPAIAT RLVG
//
