HIS1_BACSU
ID HIS1_BACSU Reviewed; 213 AA.
AC O34520;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=ATP phosphoribosyltransferase;
DE Short=ATP-PRT;
DE Short=ATP-PRTase;
DE EC=2.4.2.17;
GN Name=hisG; OrderedLocusNames=BSU34920;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lazarevic V., Soldo B., Rivolta C., Reynolds S., Mauel C., Karamata D.;
RT "Nucleotide sequence of the 300-304 chromosomal segment of Bacillus
RT subtilis.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC HisZ.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
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; AF017113; AAC67294.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15497.1; -; Genomic_DNA.
DR PIR; C69641; C69641.
DR RefSeq; NP_391372.1; NC_000964.3.
DR RefSeq; WP_009968235.1; NZ_JNCM01000033.1.
DR PDB; 2VD2; X-ray; 2.85 A; A=1-213.
DR PDBsum; 2VD2; -.
DR AlphaFoldDB; O34520; -.
DR SMR; O34520; -.
DR STRING; 224308.BSU34920; -.
DR PaxDb; O34520; -.
DR EnsemblBacteria; CAB15497; CAB15497; BSU_34920.
DR GeneID; 936568; -.
DR KEGG; bsu:BSU34920; -.
DR PATRIC; fig|224308.179.peg.3780; -.
DR eggNOG; COG0040; Bacteria.
DR InParanoid; O34520; -.
DR OMA; YVMMDYD; -.
DR PhylomeDB; O34520; -.
DR BioCyc; BSUB:BSU34920-MON; -.
DR UniPathway; UPA00031; UER00006.
DR EvolutionaryTrace; O34520; -.
DR Proteomes; UP000001570; 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; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
DR CDD; cd13595; PBP2_HisGs; 1.
DR HAMAP; MF_01018; HisG_Short; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
DR PANTHER; PTHR21403; PTHR21403; 1.
DR Pfam; PF01634; HisG; 1.
DR TIGRFAMs; TIGR00070; hisG; 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; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..213
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151898"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2VD2"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:2VD2"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:2VD2"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2VD2"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:2VD2"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:2VD2"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:2VD2"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:2VD2"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:2VD2"
FT HELIX 186..210
FT /evidence="ECO:0007829|PDB:2VD2"
SQ SEQUENCE 213 AA; 23621 MW; E4663F62A39402AD CRC64;
MGKLLTMAMP KGRIFEEAAG LLRQAGYRLP EEFEDSRKLI IDVPEENLRF ILAKPMDVTT
YVEHGVADVG IAGKDVMLEE ERDVYEVLDL NISKCHLAVA GLPNTDWSGV APRIATKYPN
VASSYFREQG EQVEIIKLNG SIELAPLIGL ADRIVDIVST GQTLKENGLV ETEHICDITS
RFIVNPVSYR MKDDVIDEMA SRLSLVVEGE TAK
