HIS1_METTH
ID HIS1_METTH Reviewed; 287 AA.
AC O27550;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=ATP phosphoribosyltransferase;
DE Short=ATP-PRT;
DE Short=ATP-PRTase;
DE EC=2.4.2.17;
GN Name=hisG; OrderedLocusNames=MTH_1506;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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 (By
CC similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Feedback inhibited by histidine. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC subfamily. {ECO:0000305}.
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; AE000666; AAB85981.1; -; Genomic_DNA.
DR PIR; H69067; H69067.
DR RefSeq; WP_010877116.1; NC_000916.1.
DR PDB; 2VD3; X-ray; 2.45 A; A/B=2-287.
DR PDBsum; 2VD3; -.
DR AlphaFoldDB; O27550; -.
DR SMR; O27550; -.
DR STRING; 187420.MTH_1506; -.
DR EnsemblBacteria; AAB85981; AAB85981; MTH_1506.
DR GeneID; 1471775; -.
DR KEGG; mth:MTH_1506; -.
DR PATRIC; fig|187420.15.peg.1469; -.
DR HOGENOM; CLU_038115_1_0_2; -.
DR OMA; YVMMDYD; -.
DR UniPathway; UPA00031; UER00006.
DR EvolutionaryTrace; O27550; -.
DR Proteomes; UP000005223; 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 HAMAP; MF_00079; HisG_Long; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR020621; ATP_PRibTrfase_HisG_long.
DR InterPro; IPR013115; HisG_C.
DR InterPro; IPR011322; N-reg_PII-like_a/b.
DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR PANTHER; PTHR21403; PTHR21403; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF08029; HisG_C; 1.
DR SUPFAM; SSF54913; SSF54913; 1.
DR TIGRFAMs; TIGR00070; hisG; 1.
DR TIGRFAMs; TIGR03455; HisG_C-term; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Glycosyltransferase; Histidine biosynthesis; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..287
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151886"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:2VD3"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 55..60
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:2VD3"
FT TURN 147..151
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 188..193
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 195..210
FT /evidence="ECO:0007829|PDB:2VD3"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 214..222
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 250..258
FT /evidence="ECO:0007829|PDB:2VD3"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:2VD3"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:2VD3"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:2VD3"
FT STRAND 275..281
FT /evidence="ECO:0007829|PDB:2VD3"
SQ SEQUENCE 287 AA; 31165 MW; EFAA5D8BF9755F48 CRC64;
MKIRIAVPSK GRISEPAIRL LENAGVGLKD TVNRKLFSKT QHPQIEVMFS RAADIPEFVA
DGAADLGITG YDLIVERGSD VEILEDLKYG RASLVLAAPE DSTIRGPEDI PRGAVIATEF
PGITENYLRE HGIDAEVVEL TGSTEIAPFI GVADLITDLS STGTTLRMNH LRVIDTILES
SVKLIANRES YATKSGIIEE LRTGIRGVID AEGKRLVMLN IDRKNLDRVR ALMPGMTGPT
VSEVLSDNGV VAVHAVVDEK EVFNLINRLK AVGARDILVV PIERIIP
