ID A0A0M2VE98_9GAMM Unreviewed; 302 AA.
AC A0A0M2VE98;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ECO:0000313|EMBL:KKO48829.1};
GN ORFNames=VT06_09970 {ECO:0000313|EMBL:KKO48829.1};
OS Arsukibacterium sp. MJ3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Arsukibacterium.
OX NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO48829.1, ECO:0000313|Proteomes:UP000034895};
RN [1] {ECO:0000313|EMBL:KKO48829.1, ECO:0000313|Proteomes:UP000034895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:KKO48829.1,
RC ECO:0000313|Proteomes:UP000034895};
RA Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J.,
RA Stougaard P., Glaring M.A.;
RT "Draft genome sequences of two protease-producing strains of
RT Arsukibacterium isolated from two cold and alkaline environments.";
RL Submitted (MAR-2015) 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}.
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:KKO48829.1}.
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DR EMBL; LAHP01000011; KKO48829.1; -; Genomic_DNA.
DR RefSeq; WP_046554156.1; NZ_LAHP01000011.1.
DR AlphaFoldDB; A0A0M2VE98; -.
DR STRING; 1632859.VT06_09970; -.
DR PATRIC; fig|1632859.4.peg.2070; -.
DR OrthoDB; 9801867at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000034895; 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; 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, 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:UP000034895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00079}.
FT DOMAIN 57..221
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 226..299
FT /note="Histidine biosynthesis HisG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08029"
SQ SEQUENCE 302 AA; 33425 MW; AC58A058338D193F CRC64;
MSPATESKRL RIAMQKSGRL SVDSQALFTS CGLKINLREQ RLIAHVENMD IDILRVRDDD
IPGLVMDGVC DLGIVGENVL EEESLQRQLD NNSYDYTVLK RLDFGGCRLS IAVPQEEEYN
GPASLEGKTI ATTYPRLLAR YLKQQSVNAR VVNLKGSVEV APRAGLADAI CDLVSTGATL
EANGLREVDV IYRSKAVLIQ RKNLTDNKHL TLIDKLMPRI NGVMQANESK YIMLHAPRAR
LDEVIALLPG AENPTMLPLA GNDQMVAIHV VSSETLFWET MEQLKVLGAS SILVLPIEKM
ME
//
