HIS1_CANAL
ID HIS1_CANAL Reviewed; 298 AA.
AC P46586; A0A1D8PP88; Q5AJZ4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=ATP phosphoribosyltransferase;
DE Short=ATP-PRT;
DE Short=ATP-PRTase;
DE EC=2.4.2.17 {ECO:0000305|PubMed:7489899};
GN Name=HIS1; OrderedLocusNames=CAALFM_C505320CA;
GN ORFNames=CaO19.11509, CaO19.4026;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 64385 / 1001;
RX PubMed=7489899; DOI=10.1016/0378-1119(95)00492-o;
RA Pla J., Perez-Diaz R.M., Navarro-Garcia F., Sanchez M., Nombela C.;
RT "Cloning of the Candida albicans HIS1 gene by direct complementation of a
RT C. albicans histidine auxotroph using an improved double-ARS shuttle
RT vector.";
RL Gene 165:115-120(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 (By
CC similarity). {ECO:0000250}.
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:0000305|PubMed:7489899};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X83871; CAA58751.1; -; Genomic_DNA.
DR EMBL; CP017627; AOW29936.1; -; Genomic_DNA.
DR PIR; S55497; S55497.
DR RefSeq; XP_721934.1; XM_716841.1.
DR AlphaFoldDB; P46586; -.
DR SMR; P46586; -.
DR STRING; 237561.P46586; -.
DR GeneID; 3636501; -.
DR KEGG; cal:CAALFM_C505320CA; -.
DR CGD; CAL0000180598; HIS1.
DR VEuPathDB; FungiDB:C5_05320C_A; -.
DR eggNOG; KOG2831; Eukaryota.
DR HOGENOM; CLU_038115_1_2_1; -.
DR InParanoid; P46586; -.
DR OMA; YVMMDYD; -.
DR OrthoDB; 842823at2759; -.
DR UniPathway; UPA00031; UER00006.
DR PRO; PR:P46586; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IGI:CGD.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IMP:CGD.
DR Gene3D; 3.30.70.120; -; 1.
DR HAMAP; MF_00079; HisG_Long; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR020621; ATP_PRibTrfase_HisG_long.
DR InterPro; IPR013115; HisG_C.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR PANTHER; PTHR21403; PTHR21403; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF08029; HisG_C; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR TIGRFAMs; TIGR00070; hisG; 1.
DR TIGRFAMs; TIGR03455; HisG_C-term; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW Histidine biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..298
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151952"
SQ SEQUENCE 298 AA; 32605 MW; FD33AF60BBFE3A0F CRC64;
MDLVNHLPDR LLFAVPKKGR LYEKCCNLLS GADIQFRRSN RLDIALSTNL PIALIFLPAA
DIPVFVGEGN CDLGITGLDQ IKEAEQFDNI EDLLDLKFGS CKLQIQVPAD GEYEKPEQLV
GKKIVSSFTK LSTDYFKQLS DKPTNIRYVG GSVEASCALG VADAIVDLVE SGETMKAAGL
KAIETILETS AHLISSKKSK FPEMVNIIVQ RLQGVLAAQE YVLCNYNAPK SIQAKCLTIT
PGRRAATVST LDKHSDDEED WVAISSMVNR KEIGNVMDEL KKAGATDILV LEISNCRV
