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Database: UniProt
Entry: A0A1H7ZLL2_9FIRM
LinkDB: A0A1H7ZLL2_9FIRM
Original site: A0A1H7ZLL2_9FIRM 
ID   A0A1H7ZLL2_9FIRM        Unreviewed;       486 AA.
AC   A0A1H7ZLL2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ORFNames=SAMN05216180_0752 {ECO:0000313|EMBL:SEM59215.1};
OS   Hydrogenoanaerobacterium saccharovorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Hydrogenoanaerobacterium.
OX   NCBI_TaxID=474960 {ECO:0000313|EMBL:SEM59215.1, ECO:0000313|Proteomes:UP000199158};
RN   [1] {ECO:0000313|EMBL:SEM59215.1, ECO:0000313|Proteomes:UP000199158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.5070 {ECO:0000313|EMBL:SEM59215.1,
RC   ECO:0000313|Proteomes:UP000199158};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOCG01000001; SEM59215.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7ZLL2; -.
DR   STRING; 474960.SAMN05216180_0752; -.
DR   OrthoDB; 9770610at2; -.
DR   UniPathway; UPA00253; UER00457.
DR   Proteomes; UP000199158; 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; IPR041619; NAPRTase_C.
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:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   Pfam; PF17956; NAPRTase_C; 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:SEM59215.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000199158};
KW   Transferase {ECO:0000256|RuleBase:RU365100, ECO:0000313|EMBL:SEM59215.1}.
FT   DOMAIN          13..137
FT                   /note="Nicotinate phosphoribosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17767"
FT   DOMAIN          158..339
FT                   /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF04095"
FT   DOMAIN          367..476
FT                   /note="Nicotinate phosphoribosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17956"
SQ   SEQUENCE   486 AA;  55208 MW;  CE279E8061722AE3 CRC64;
     MEFQGSKDRN LTMLVDFYEI TMANGYLEQG IGDRIAVFDM FFRKIPDGGG FALFAGLEQL
     IDYLNNLSFT HDDIEYLRSR KIFCDEFLDY LANFKFECDV WSVQEGTPVF PNEPIVIVRG
     PIIQAQLIET MTLLTINHQS LVTTKANRIV RAAQGRGISE FGSRRAQSYD AAILGARAAY
     IGGCTGTACV MSDRLYGVPA VGTMAHSWVQ MFDSEYDAFK KYAEIYPENC IVLVDTYNVI
     KSGVPNAIKM FNEVLLPMGY RPKGIRIDSG DIAYLSKKAR VMLDEAGFSD VEICASNSLD
     EYLIRDLLIQ DAKVDSFGVG ENLITSKSDP VFGGVYKLAA IQNDDGSYTP KIKISETIEK
     ITNPHFKTIY RFYNKSNGQA IADCVTLFDE VIDDNKPYTI FDPVATWKKK TLTNFTIRKL
     LIPIFEKGKL VYECPALEDI RSYCEEQVSL LWDEVKRFEF PHRYYVDLSD KLWKIKNEML
     SKYNFG
//
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