ID G7DUN3_MIXOS Unreviewed; 1514 AA.
AC G7DUN3;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU003838};
DE EC=6.3.4.21 {ECO:0000256|ARBA:ARBA00013236, ECO:0000256|RuleBase:RU003838};
GN Name=Mo00942 {ECO:0000313|EMBL:GAA94293.1};
GN ORFNames=E5Q_00942 {ECO:0000313|EMBL:GAA94293.1};
OS Mixia osmundae (strain CBS 9802 / IAM 14324 / JCM 22182 / KY 12970).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina; Mixiomycetes;
OC Mixiales; Mixiaceae; Mixia.
OX NCBI_TaxID=764103 {ECO:0000313|EMBL:GAA94293.1, ECO:0000313|Proteomes:UP000009131};
RN [1] {ECO:0000313|Proteomes:UP000009131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 9802 / IAM 14324 / JCM 22182 / KY 12970
RC {ECO:0000313|Proteomes:UP000009131};
RX PubMed=21478649; DOI=10.2323/jgam.57.63;
RA Nishida H., Nagatsuka Y., Sugiyama J.;
RT "Draft genome sequencing of the enigmatic basidiomycete Mixia osmundae.";
RL J. Gen. Appl. Microbiol. 57:63-67(2011).
CC -!- FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide
CC from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of
CC ATP. {ECO:0000256|RuleBase:RU003838}.
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:RU003838};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004952, ECO:0000256|RuleBase:RU003838}.
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:RU003838}.
CC -!- SIMILARITY: Belongs to the NAPRTase family.
CC {ECO:0000256|ARBA:ARBA00010897, ECO:0000256|RuleBase:RU003838}.
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:GAA94293.1}.
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DR EMBL; BABT02000029; GAA94293.1; -; Genomic_DNA.
DR RefSeq; XP_014564938.1; XM_014709452.1.
DR STRING; 764103.G7DUN3; -.
DR GeneID; 26269507; -.
DR eggNOG; KOG2511; Eukaryota.
DR HOGENOM; CLU_248050_0_0_1; -.
DR InParanoid; G7DUN3; -.
DR OrthoDB; 1333333at2759; -.
DR UniPathway; UPA00253; UER00457.
DR Proteomes; UP000009131; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; 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; 3.20.140.10; nicotinate phosphoribosyltransferase; 1.
DR HAMAP; MF_00570; NAPRTase; 1.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR006406; Nic_PRibTrfase.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR NCBIfam; TIGR01514; NAPRTase; 1.
DR PANTHER; PTHR11098; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR11098:SF1; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17767; NAPRTase_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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU003838};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Pyridine nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022642,
KW ECO:0000256|RuleBase:RU003838};
KW Reference proteome {ECO:0000313|Proteomes:UP000009131};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 870..890
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..933
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 978..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1018
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1030..1048
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1085..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1130..1150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..137
FT /note="Nicotinate phosphoribosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17767"
FT DOMAIN 171..420
FT /note="Nicotinate/nicotinamide phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF04095"
FT REGION 456..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1514 AA; 166734 MW; 60CC6197CBF27692 CRC64;
MTMADYPVSL IDTDLYKLTM SQFVYRLYPD VQVSYKFTNR TSDRTFTKQA FAWIEDKINA
LESLRLTTEE KGWLSRLPFF QSDYLDWLAT FQLRPREQIK LAWQPISNSD KGAIDLEIRG
TWLDTILYEV PIISIISQGY FLHVDKDWDL VGQKALAYSK AERLIKNGCI FSDFGARRRR
SYQSQEIVLR GLMAAQADLQ DKGFKGKFSG CSNAHFAHKL GLTPVGTLAH ELFMAIGAMQ
GLEKANTLVL EQWETVYPNG QLSIALTDTF TSAAFFEAFV GEPARVQRWT GLRQDSGDPF
AFIPLAIEAY RKADIDFSNK VIVFSDSLDI DKAVRLQKAS EEAGIRCSFG IGTYFTNDFV
AVASDSRDPA SYGEGNIRQG EPSTALNIVI KLATADGKPC VKISDETSKI TGTAEAVEAA
KRLCSRLPER SSLSLHEPTT PAEKIIREAL LPTAPRKGRT GLSAKEASQT AGVSPSSVHQ
SGETVEIVAY AGSEQSAEEQ RNVSLKRIVN LIRRDRVDSG TSSETSAISA LTNRERLIIS
KWLYEVDVRP ASGGWLRVPH EARWLANRMF SRLAARCASA HDNRSRSSAL WLLATACLSL
SCKFILDFSE PLVSLELRWF ATICPAANTR MHHLAVIERE LLALGGYAIL TQPTPQAYGD
EIYNTVPELQ QLSLTQASVW SSIGRRFHHN IRLFTHDAGF SSTTVGQMTL VALIEASADQ
APDLISLRSS LLGVIPLAQD ELDSGMRTKL FFGAAQLTLR DQRHVQQEDV AASMGSYSLL
STSLSSEKSP GSHTNGYSPS HSVRLSPTAS RDPTTLPAKV VRLVLGSYGP LLASAYVAAS
AHSSLAIYKG ASLLGYHFLF RQGCDVYKLL FPWLLVASVP AVFVQVYMAY SSTTDEQQRG
LVLLKDIVLS LISWRVALAG ILKAIWLASS IFAATRLDFP TWISFKALSV CLVISLRSHR
ENFEAGNGYR DVTRATKTIV LLVGALTVSL LLVSRVYAGG TFLALCAACC EAASILLLNG
ESQCVGRRPF SFVPFVLGFG IVVAALRIHG MQAYNREIAD GPHAYLADRN VPVLADLQQW
ASLEVGLFVL LAPLAVIAAW PAATVLPANA YAIVISALQH ALPSSVSTQL AGLLVIAQAL
PVYTVLVTSF SQMPKTPNAS EEFLDFGERP ARQTRLEQAS SIASATRQRL LVLLDSARSV
LASGPSQQLW PALATLLIAA LLPVALWTTR AWVNGYDDSL DVVVAYYDEP LDRIHVLWAA
LNAAPAIYLR NPKLHLYVKA PDANLTALAM EYHPHKLQQL ENRGREGGTY LSHILQHYDA
TERWLNPDIP RSRSAQHSGA MAKHTIFLQA HLGWNNMAGA RFALLRQNTR FMSFGPYIEM
KDGVEGYLGN GLEIPGFDDI YQIFVGHGWQ GGSSQLASWS AQVVASREAI MRNAQSAYKK
ILSQVTADHA SPDIQVPPWW DHKKGDPSDP WFGHAVERAW PIIFGCDEYQ IAFDCDFEAS
DPALCACYDG PRYQ
//
