ID A0A1Q5D5U0_9ACTN Unreviewed; 282 AA.
AC A0A1Q5D5U0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998, ECO:0000256|HAMAP-Rule:MF_00079};
DE Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_00079};
DE Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_00079};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946, ECO:0000256|HAMAP-Rule:MF_00079};
GN Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079};
GN ORFNames=AMK10_30095 {ECO:0000313|EMBL:OKI91141.1};
OS Streptomyces sp. CB02058.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703921 {ECO:0000313|EMBL:OKI91141.1, ECO:0000313|Proteomes:UP000185610};
RN [1] {ECO:0000313|EMBL:OKI91141.1, ECO:0000313|Proteomes:UP000185610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02058 {ECO:0000313|EMBL:OKI91141.1,
RC ECO:0000313|Proteomes:UP000185610};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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 HisG enzymatic activity.
CC {ECO:0000256|ARBA:ARBA00024861, ECO:0000256|HAMAP-Rule:MF_00079}.
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, ECO:0000256|HAMAP-
CC Rule:MF_00079};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00079};
CC -!- ACTIVITY REGULATION: Feedback inhibited by histidine.
CC {ECO:0000256|HAMAP-Rule:MF_00079}.
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, ECO:0000256|HAMAP-Rule:MF_00079}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC subfamily. {ECO:0000256|ARBA:ARBA00007955, ECO:0000256|HAMAP-
CC Rule:MF_00079}.
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:OKI91141.1}.
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DR EMBL; LIPG01000006; OKI91141.1; -; Genomic_DNA.
DR RefSeq; WP_073751810.1; NZ_LIPG01000006.1.
DR AlphaFoldDB; A0A1Q5D5U0; -.
DR OrthoDB; 9801867at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000185610; Unassembled WGS sequence.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd13591; PBP2_HisGL1; 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00079}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00079};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_00079}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00079};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00079}.
FT DOMAIN 49..203
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 207..278
FT /note="Histidine biosynthesis HisG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08029"
SQ SEQUENCE 282 AA; 30572 MW; B45038F1AA8F4067 CRC64;
MLRIAVPNKG SLSGPAMAML HEAGYQQRKE SKELVLVDPT NEVEFFYLRP RDIAIYVSSG
RLDIGITGRD LLLDSGADAE EILQLGFARS TFRYATKPGT AEGPQDFDGM TIATSYEGIV
GAHLAEAGVK ASVVHLDGAV ETAIELGVAQ VIADVVETGT SLRNAGLEVI GEPIMTSEAV
VIRRKGADAE DPKVQQFLRR LQGVLVARTY VMMDYDCRVE HLERAVALTP GLESPTISPL
HHEGWVAVRS MVASKEAQRI MDDLYELGAR AILTTAIHAC RL
//
