PNCB_AGRFC
ID PNCB_AGRFC Reviewed; 434 AA.
AC Q8UIS9;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Nicotinate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00570};
DE Short=NAPRTase {ECO:0000255|HAMAP-Rule:MF_00570};
DE EC=6.3.4.21 {ECO:0000255|HAMAP-Rule:MF_00570};
GN Name=pncB {ECO:0000255|HAMAP-Rule:MF_00570}; OrderedLocusNames=Atu0213;
GN ORFNames=AGR_C_367;
OS Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS (strain C58)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=176299;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743193; DOI=10.1126/science.1066804;
RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA Gordon M.P., Olson M.V., Nester E.W.;
RT "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT C58.";
RL Science 294:2317-2323(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C58 / ATCC 33970;
RX PubMed=11743194; DOI=10.1126/science.1066803;
RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT "Genome sequence of the plant pathogen and biotechnology agent
RT Agrobacterium tumefaciens C58.";
RL Science 294:2323-2328(2001).
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:0000255|HAMAP-Rule:MF_00570}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00570};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00570}.
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:0000255|HAMAP-Rule:MF_00570}.
CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000255|HAMAP-
CC Rule:MF_00570}.
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DR EMBL; AE007869; AAK86031.2; -; Genomic_DNA.
DR PIR; AF2602; AF2602.
DR PIR; F97384; F97384.
DR RefSeq; NP_353246.2; NC_003062.2.
DR RefSeq; WP_010970734.1; NC_003062.2.
DR PDB; 1YBE; X-ray; 2.50 A; A/B=1-434.
DR PDBsum; 1YBE; -.
DR AlphaFoldDB; Q8UIS9; -.
DR SMR; Q8UIS9; -.
DR STRING; 176299.Atu0213; -.
DR PRIDE; Q8UIS9; -.
DR DNASU; 1132251; -.
DR EnsemblBacteria; AAK86031; AAK86031; Atu0213.
DR KEGG; atu:Atu0213; -.
DR PATRIC; fig|176299.10.peg.204; -.
DR eggNOG; COG1488; Bacteria.
DR HOGENOM; CLU_030991_1_0_5; -.
DR OMA; QAVFHRY; -.
DR PhylomeDB; Q8UIS9; -.
DR UniPathway; UPA00253; UER00457.
DR EvolutionaryTrace; Q8UIS9; -.
DR Proteomes; UP000000813; Chromosome circular.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR11098; PTHR11098; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR01514; NAPRTase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Ligase; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW Reference proteome.
FT CHAIN 1..434
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000205817"
FT MOD_RES 242
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00570"
FT HELIX 2..7
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1YBE"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 141..157
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 162..183
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1YBE"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 243..251
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 255..272
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 296..300
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 311..324
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:1YBE"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:1YBE"
FT STRAND 386..393
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1YBE"
FT HELIX 412..422
FT /evidence="ECO:0007829|PDB:1YBE"
SQ SEQUENCE 434 AA; 49902 MW; ABC37DD605AE647F CRC64;
MTKTDIATRV HNHTWKLDPI VRSLIDTDFY KLLMLQMIWK LYPEVDATFS LINRTKTVRL
AEEIDEMELR EQLDHARTLR LSKKENIWLA GNTFYGRSQI FEPEFLSWLS SYQLPEYELF
KRDGQYELNF HGRWMDTTLW EIPALSIINE LRSRSAMRSL GYFTLDVLYA RAKAKMWEKV
ERLRELPGLR ISDFGTRRRH SFLWQRWCVE ALKEGIGPAF TGTSNVLLAM DSDLEAVGTN
AHELPMVVAA LAQTNEELAA APYQVLKDWN RLYGGNLLIV LPDAFGTAAF LRNAPEWVAD
WTGFRPDSAP PIEGGEKIIE WWRKMGRDPR TKMLIFSDGL DVDAIVDTYR HFEGRVRMSF
GWGTNLTNDF AGCAPKTIAS LKPISIVCKV SDANGRPAVK LSDNPQKATG DPAEVERYLK
FFGEEDHKEQ KVLV
