HIS1_MYCTU
ID HIS1_MYCTU Reviewed; 284 AA.
AC P9WMN1; L0TBL0; O33256; P60759;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 38.
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, ECO:0000303|PubMed:12511575};
DE EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_00079, ECO:0000305|PubMed:12511575};
GN Name=hisG {ECO:0000303|PubMed:12511575}; OrderedLocusNames=Rv2121c;
GN ORFNames=MTCY261.17c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3] {ECO:0007744|PDB:1NH7, ECO:0007744|PDB:1NH8}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF NATIVE PROTEIN AND IN COMPLEX WITH
RP HISTIDINE AND AMP, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12511575; DOI=10.1074/jbc.m212124200;
RA Cho Y., Sharma V., Sacchettini J.C.;
RT "Crystal structure of ATP phosphoribosyltransferase from Mycobacterium
RT tuberculosis.";
RL J. Biol. Chem. 278:8333-8339(2003).
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, ECO:0000305|PubMed:12511575};
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. Also inhibited by
CC AMP. {ECO:0000269|PubMed:12511575}.
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 -!- SUBUNIT: Equilibrium between an active dimeric form, an inactive
CC hexameric form and higher aggregates. Interconversion between the
CC various forms is largely reversible and is influenced by the natural
CC substrates and inhibitors of the enzyme. {ECO:0000255|HAMAP-
CC Rule:MF_00079, ECO:0000269|PubMed:12511575}.
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; AL123456; CCP44896.1; -; Genomic_DNA.
DR PIR; D70513; D70513.
DR RefSeq; NP_216637.1; NC_000962.3.
DR RefSeq; WP_003411047.1; NZ_NVQJ01000058.1.
DR PDB; 1NH7; X-ray; 2.70 A; A=1-284.
DR PDB; 1NH8; X-ray; 1.80 A; A=1-284.
DR PDB; 5LHT; X-ray; 2.06 A; A=1-284.
DR PDB; 5LHU; X-ray; 2.02 A; A=1-284.
DR PDB; 5U99; X-ray; 2.40 A; A=1-284.
DR PDBsum; 1NH7; -.
DR PDBsum; 1NH8; -.
DR PDBsum; 5LHT; -.
DR PDBsum; 5LHU; -.
DR PDBsum; 5U99; -.
DR AlphaFoldDB; P9WMN1; -.
DR SMR; P9WMN1; -.
DR STRING; 83332.Rv2121c; -.
DR BindingDB; P9WMN1; -.
DR ChEMBL; CHEMBL6086; -.
DR DrugCentral; P9WMN1; -.
DR PaxDb; P9WMN1; -.
DR DNASU; 888689; -.
DR GeneID; 45426096; -.
DR GeneID; 888689; -.
DR KEGG; mtu:Rv2121c; -.
DR TubercuList; Rv2121c; -.
DR eggNOG; COG0040; Bacteria.
DR OMA; YVMMDYD; -.
DR PhylomeDB; P9WMN1; -.
DR BRENDA; 2.4.2.17; 3445.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0016208; F:AMP binding; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IDA:MTBBASE.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0000105; P:histidine biosynthetic process; IDA:MTBBASE.
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..284
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151857"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1NH8"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1NH7"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 160..164
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 167..177
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 195..209
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1NH8"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:1NH8"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:1NH8"
SQ SEQUENCE 284 AA; 30481 MW; C248C57399302B2A CRC64;
MLRVAVPNKG ALSEPATEIL AEAGYRRRTD SKDLTVIDPV NNVEFFFLRP KDIAIYVGSG
ELDFGITGRD LVCDSGAQVR ERLALGFGSS SFRYAAPAGR NWTTADLAGM RIATAYPNLV
RKDLATKGIE ATVIRLDGAV EISVQLGVAD AIADVVGSGR TLSQHDLVAF GEPLCDSEAV
LIERAGTDGQ DQTEARDQLV ARVQGVVFGQ QYLMLDYDCP RSALKKATAI TPGLESPTIA
PLADPDWVAI RALVPRRDVN GIMDELAAIG AKAILASDIR FCRF
