ID G7HWN4_9CORY Unreviewed; 457 AA.
AC G7HWN4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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:CCE54599.1};
GN ORFNames=CCAS_05135 {ECO:0000313|EMBL:CCE54599.1};
OS Corynebacterium casei UCMA 3821.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1110505 {ECO:0000313|EMBL:CCE54599.1, ECO:0000313|Proteomes:UP000004840};
RN [1] {ECO:0000313|EMBL:CCE54599.1, ECO:0000313|Proteomes:UP000004840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCMA 3821 {ECO:0000313|EMBL:CCE54599.1,
RC ECO:0000313|Proteomes:UP000004840};
RX PubMed=22247534; DOI=10.1128/JB.06496-11;
RA Monnet C., Loux V., Bento P., Gibrat J.F., Straub C., Bonnarme P.,
RA Landaud S., Irlinger F.;
RT "Genome Sequence of Corynebacterium casei UCMA 3821, Isolated from a Smear-
RT Ripened Cheese.";
RL J. Bacteriol. 194:738-739(2012).
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:CCE54599.1}.
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DR EMBL; CAFW01000036; CCE54599.1; -; Genomic_DNA.
DR RefSeq; WP_006822123.1; NZ_CAFW01000036.1.
DR AlphaFoldDB; G7HWN4; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000004840; 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 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:CCE54599.1};
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:CCE54599.1}.
FT DOMAIN 30..151
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 173..363
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
SQ SEQUENCE 457 AA; 49328 MW; 0BE042F6B0EBAEDA CRC64;
MELNGTEKPC RALDLFAVNP KTNQPQSTAL LTDMYELTML QAALADGTAE RPVVCEVFAR
RLSNERRYGV VAGIPRVLDA VMNFRFTEEQ LATLTFLDDA TRDYLRNYRF SGQIDGYREG
ELYFPNSPLL TVRGTFGEAI LLETVILSIM NSDSAVASAA SRMVVSADGR PIIEMGSRRT
NEQAAVTAAR AAYLAGFQST SNLEAAARFG IPASGTAAHS WTLAHVNDDG SANEKAAFKS
QIEAHGVGTT LLVDTFDITQ GVNNAIEVAG IELGGVRIDS GNLGAITRRV RKQLDDLGAH
NTKIVVSSDL DEFAIAGLRG DPVDVYGVGT SVVTGSGAPT ASMVYKIVEV DGHPVAKRSE
SKKSVGGAKR AIRSYRSSGV AIEEIIFPFH ENEPDTGHLT SKMLTVPLIR DGEIVEGQPT
LDESREYLAQ NIKTLPWEGL ALTRDEPAVH TRYVGFE
//
