ID L0JFH3_NATP1 Unreviewed; 285 AA.
AC L0JFH3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:ELY70207.1};
GN OrderedLocusNames=Natpe_0117 {ECO:0000313|EMBL:AGB30059.1};
GN ORFNames=C488_19377 {ECO:0000313|EMBL:ELY70207.1};
OS Natrinema pellirubrum (strain DSM 15624 / CIP 106293 / JCM 10476 / NCIMB
OS 786 / 157).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=797303 {ECO:0000313|EMBL:AGB30059.1, ECO:0000313|Proteomes:UP000010843};
RN [1] {ECO:0000313|EMBL:AGB30059.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 15624 {ECO:0000313|EMBL:AGB30059.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000010843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 / JCM 10476 / NCIMB 786
RC {ECO:0000313|Proteomes:UP000010843};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Sproer C., Anderson I., Woyke T.;
RT "Complete sequence of chromosome of Natrinema pellirubrum DSM 15624.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000011593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 {ECO:0000313|Proteomes:UP000011593};
RA Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D., Darling A.,
RA Eisen J.A., Facciotti M.T.;
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ELY70207.1, ECO:0000313|Proteomes:UP000011593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15624 {ECO:0000313|EMBL:ELY70207.1,
RC ECO:0000313|Proteomes:UP000011593};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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|HAMAP-Rule:MF_00079}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003372; AGB30059.1; -; Genomic_DNA.
DR EMBL; AOIE01000113; ELY70207.1; -; Genomic_DNA.
DR RefSeq; WP_006183214.1; NZ_AOIE01000113.1.
DR AlphaFoldDB; L0JFH3; -.
DR STRING; 797303.Natpe_0117; -.
DR GeneID; 14336034; -.
DR KEGG; npe:Natpe_0117; -.
DR PATRIC; fig|797303.5.peg.3859; -.
DR eggNOG; arCOG02208; Archaea.
DR HOGENOM; CLU_038115_1_0_2; -.
DR OrthoDB; 33116at2157; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000010843; Chromosome.
DR Proteomes; UP000011593; 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 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:SF10; 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|ARBA:ARBA00022490, 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|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00079}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00079}.
FT DOMAIN 49..199
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
FT DOMAIN 207..282
FT /note="Histidine biosynthesis HisG C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08029"
SQ SEQUENCE 285 AA; 30641 MW; 73B644D7EAEC4AD9 CRC64;
MRIAVPNKGR LHEPTIDLLE RAGLHLENGA DRKLYADTVD PDVTVLFARA ADIPEYVADG
AADLGITGFD QVQEARVDNV SELLDLEFGR CRLVLAAPED GDTNSVADLT GKTVATEFPN
ITADFFADTG VDPDIVEVSG ATELTPHVEM ADAIVDITST GTTLKMNRLA VVEEVLASSV
RLFGREDVLD DPKVDEVRTA LGSVKQAEGK RYLMMNVPQD RLEAVRDVIP GLGGPTVMDI
ADDEDGEKVA VHAVVDESDV FETITAVKEA GASDILVTEI ERLVE
//
