ID F8A6B3_CELGA Unreviewed; 282 AA.
AC F8A6B3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=Celgi_1762 {ECO:0000313|EMBL:AEI12269.1};
OS Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI12269.1, ECO:0000313|Proteomes:UP000000485};
RN [1] {ECO:0000313|Proteomes:UP000000485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP002665; AEI12269.1; -; Genomic_DNA.
DR RefSeq; WP_013883788.1; NC_015671.1.
DR AlphaFoldDB; F8A6B3; -.
DR STRING; 593907.Celgi_1762; -.
DR KEGG; cga:Celgi_1762; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_1_1_11; -.
DR OrthoDB; 9801867at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000485; Chromosome.
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; 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, 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 Reference proteome {ECO:0000313|Proteomes:UP000000485};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00079}.
FT DOMAIN 49..202
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; 30514 MW; 3135765DD8199204 CRC64;
MLRIAVPNKG SLSEPAAEML REAGYRQRRD SRELVLPDPD NDVEFFFLRP RDIAVYVGAG
TVDVGITGRD LLLDSESAAV EHLPLGFARS TFRFATTAGA MTDIAQIEGQ RVATSYPVLV
RRSLAERGVT PSAVVRLDGA VETAIRLGVA DVIADVVETG STLRAAGLEI FGEPLLRSEA
VLARRADVAA PAGLEVLTRR LQGVLTARQY VLMDYDVPLS LVDAAVAVTP GLESPTVSPL
HNRDWAAVRA MVRRDETNRV MDQLYDLGAR AILVTSIHAC RL
//
