ID W6Z1L7_COCMI Unreviewed; 345 AA.
AC W6Z1L7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN ORFNames=COCMIDRAFT_29710 {ECO:0000313|EMBL:EUC41539.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC41539.1};
RN [1] {ECO:0000313|EMBL:EUC41539.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC41539.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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}.
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DR EMBL; KI964098; EUC41539.1; -; Genomic_DNA.
DR RefSeq; XP_007691947.1; XM_007693757.1.
DR AlphaFoldDB; W6Z1L7; -.
DR STRING; 930090.W6Z1L7; -.
DR GeneID; 19121556; -.
DR KEGG; bor:COCMIDRAFT_29710; -.
DR eggNOG; KOG2831; Eukaryota.
DR HOGENOM; CLU_038115_1_2_1; -.
DR OrthoDB; 275532at2759; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000054032; 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 CDD; cd13592; PBP2_HisGL2; 1.
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 Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 88..263
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 268..340
FT /note="Histidine biosynthesis HisG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08029"
SQ SEQUENCE 345 AA; 36868 MW; 6693BDD28FA56D45 CRC64;
MGFLVGVNGT LDEVAHRPRQ GSRSLPFMTD LLGNSLNDRL LFAVPKKGRL HQACLDLLHG
SDIQFHRHSR LDIALVKNLP LALVFLPAAD IPTFVGEGRV DLGITGRDQV AEHECVTPPT
ATTGVDEVLD LGFGKCSLQV QVPAKGDLTK PEDLIGKNVV TSFTNLAEQY FRKLEAEQAG
TTNGETNGDA KLKTVIKYVG GSVEAACALG VADGIVDLVE SGETMRAAGL KAISTVVTSS
AILIKSKHPS DPKLVDLITA RIKGVITAQK YVLCTYNVPR SKLDAARTIT PGRRAPTVNA
LEEDGWVAVQ AMVLRKDIAI AMDKLTEVGA TDLIVTKIEN SRTGD
//
