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Database: UniProt
Entry: HIS1_METMP
LinkDB: HIS1_METMP
Original site: HIS1_METMP 
ID   HIS1_METMP              Reviewed;         288 AA.
AC   P60807;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   13-SEP-2023, entry version 104.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_00079};
DE            EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_00079};
GN   Name=hisG {ECO:0000255|HAMAP-Rule:MF_00079}; OrderedLocusNames=MMP0947;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00079};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00079};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by histidine.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00079}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00079}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00079}.
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DR   EMBL; BX950229; CAF30503.1; -; Genomic_DNA.
DR   RefSeq; WP_011170891.1; NC_005791.1.
DR   AlphaFoldDB; P60807; -.
DR   SMR; P60807; -.
DR   STRING; 267377.MMP0947; -.
DR   EnsemblBacteria; CAF30503; CAF30503; MMP0947.
DR   GeneID; 41279457; -.
DR   KEGG; mmp:MMP0947; -.
DR   PATRIC; fig|267377.15.peg.975; -.
DR   eggNOG; arCOG02208; Archaea.
DR   HOGENOM; CLU_038115_1_0_2; -.
DR   OMA; YVMMDYD; -.
DR   OrthoDB; 33116at2157; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000590; 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   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: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.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Glycosyltransferase;
KW   Histidine biosynthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..288
FT                   /note="ATP phosphoribosyltransferase"
FT                   /id="PRO_0000151885"
SQ   SEQUENCE   288 AA;  31561 MW;  5EA9B4CAB3779ED2 CRC64;
     MILLALPNKG RISKPVNEIL EKSGLKISVH GRSLFAKTVD PEIKVMFARA KDIPEFVRDG
     VADVGVTGYD LMLERDTEEE LEMLLDFKFG NARLVLAAPE NSDVNSIEDV KNGMKIATEF
     PGLTKRYLEK KGLNLEIIEL SGATEIAPFI GVSDLICDLT STGTTLQLNR LKEIENVVSS
     STRLVANKKS MEDPEKSAKI NQVLSGIKSV MYAQSKRLIM MNAPKDKVSE ITSVIPGMGG
     PTVSEILSNC NMLAINAVID ENKVFETVSN LEKLGARDIL VVPIERIL
//
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