ID A0A2H0ZE38_CANAR Unreviewed; 304 AA.
AC A0A2H0ZE38;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN ORFNames=B9J08_005247 {ECO:0000313|EMBL:PIS48553.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS48553.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS48553.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS48553.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial
CC role in the pathway because the rate of histidine biosynthesis seems to
CC be controlled primarily by regulation of the enzymatic activity.
CC {ECO:0000256|ARBA:ARBA00024646}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:73183; EC=2.4.2.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000915};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC {ECO:0000256|ARBA:ARBA00004667}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009372}.
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:PIS48553.1}.
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DR EMBL; PEKT02000010; PIS48553.1; -; Genomic_DNA.
DR STRING; 498019.A0A2H0ZE38; -.
DR EnsemblFungi; B9J08_005247-t37_1; B9J08_005247-t37_1-p1; B9J08_005247.
DR VEuPathDB; FungiDB:B9J08_005247; -.
DR VEuPathDB; FungiDB:CJI96_0004033; -.
DR VEuPathDB; FungiDB:CJI97_005329; -.
DR VEuPathDB; FungiDB:CJJ07_001895; -.
DR VEuPathDB; FungiDB:CJJ09_004109; -.
DR VEuPathDB; FungiDB:QG37_03727; -.
DR OMA; YVMMDYD; -.
DR OrthoDB; 275532at2759; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000230249; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.120; -; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR HAMAP; MF_00079; HisG_Long; 1.
DR InterPro; IPR020621; ATP-PRT_HisG_long.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR013115; HisG_C.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR NCBIfam; TIGR00070; hisG; 1.
DR NCBIfam; TIGR03455; HisG_C-term; 1.
DR PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF08029; HisG_C; 1.
DR SUPFAM; SSF54913; GlnB-like; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:PIS48553.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Reference proteome {ECO:0000313|Proteomes:UP000230249};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIS48553.1}.
FT DOMAIN 59..206
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 224..301
FT /note="Histidine biosynthesis HisG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08029"
SQ SEQUENCE 304 AA; 33347 MW; 3FF50EF418EFC134 CRC64;
MDLVNHLPDR LMFAVPKKGR LYEKCCNFLA GADIHFRRSN RLDIALSTNL PIALIFLPAA
DIPTFVGEGK CDLGITGLDQ VKEAEMLSSV ELLLDLQFGK CKLQVQVPEK GEYTKPEELV
GKKIVTSFTN LAGTFFSDLE KAQGVQEKKT NIRYVGGSVE ASCALGVGDA IVDLVESGET
MKAAGLKPIA TILETSAQLI VSKKPRFPDL VKIIHQRFEG IMAAQRYVLC TYNAPRSIVP
EVLKITPGRR AATISALENQ EMSDEPWVAI SSMVEKARIS DVMDELKKCG GTDILVFDIN
NCRV
//
