ID A0A0P8A6Y1_9RHOB Unreviewed; 239 AA.
AC A0A0P8A6Y1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998};
DE EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946};
GN Name=hisG {ECO:0000313|EMBL:KPP89877.1};
GN ORFNames=HLUCCA05_06870 {ECO:0000313|EMBL:KPP89877.1};
OS Roseibaca calidilacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Roseibaca.
OX NCBI_TaxID=1666912 {ECO:0000313|EMBL:KPP89877.1, ECO:0000313|Proteomes:UP000050413};
RN [1] {ECO:0000313|EMBL:KPP89877.1, ECO:0000313|Proteomes:UP000050413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-91 {ECO:0000313|EMBL:KPP89877.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-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}.
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 -!- 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:KPP89877.1}.
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DR EMBL; LJSG01000020; KPP89877.1; -; Genomic_DNA.
DR RefSeq; WP_072245706.1; NZ_FBYC01000004.1.
DR AlphaFoldDB; A0A0P8A6Y1; -.
DR STRING; 1666912.Ga0058931_1416; -.
DR PATRIC; fig|1666912.4.peg.203; -.
DR OrthoDB; 9806435at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000050413; 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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR NCBIfam; TIGR00070; hisG; 1.
DR PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR Pfam; PF01634; HisG; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:KPP89877.1};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KPP89877.1}.
FT DOMAIN 54..227
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 239 AA; 25729 MW; 2299983F140600FB CRC64;
MTLKLGVPSK GRLMEQSFDW FTERGLTLAR TGSAREYAGA VEGVDGVELV LLSASEIPRE
LAAGRIHLGV TGSDLVRESL PDWAASVAEL APMGFGNADL ILAVPVTWVD VETLDDLDAA
AAAFRARHGF RLRIATKYHR LVREHLRAHG VADYQLVDSQ GATEGTIRNL TAEAVADITT
TGETLRANHL KILQGAPIHR SQATLFASRI ALWGPASAAL KQLAHKLDLA LPDGFLPNR
//
