HIS1_PSYA2
ID HIS1_PSYA2 Reviewed; 231 AA.
AC Q4FQF7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01018};
DE Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_01018};
DE Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_01018};
DE EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_01018};
GN Name=hisG {ECO:0000255|HAMAP-Rule:MF_01018}; OrderedLocusNames=Psyc_1903;
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX PubMed=20154119; DOI=10.1128/aem.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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_01018}.
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_01018};
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_01018}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01018}.
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:0000255|HAMAP-Rule:MF_01018}.
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DR EMBL; CP000082; AAZ19751.1; -; Genomic_DNA.
DR RefSeq; WP_011281160.1; NC_007204.1.
DR PDB; 5M8H; X-ray; 2.34 A; E/F/G/H=1-231.
DR PDB; 6FCA; X-ray; 2.09 A; A=1-231.
DR PDB; 6FCC; X-ray; 1.89 A; A=1-231.
DR PDB; 6FCT; X-ray; 1.89 A; A=1-231.
DR PDB; 6FCW; X-ray; 2.00 A; A=1-231.
DR PDB; 6FCY; X-ray; 1.96 A; A=1-231.
DR PDB; 6FD9; X-ray; 2.20 A; A=1-231.
DR PDB; 6FTT; X-ray; 2.29 A; E/F/G/H=1-231.
DR PDB; 6FU2; X-ray; 2.71 A; C/D=1-231.
DR PDB; 6FU7; X-ray; 2.31 A; C/D=1-231.
DR PDB; 6FUA; X-ray; 2.80 A; C/D=1-231.
DR PDB; 6R02; X-ray; 2.65 A; E/F/G/H=1-231.
DR PDB; 7Z6R; X-ray; 2.55 A; C/D=1-231.
DR PDB; 7Z8U; X-ray; 2.00 A; A=1-231.
DR PDBsum; 5M8H; -.
DR PDBsum; 6FCA; -.
DR PDBsum; 6FCC; -.
DR PDBsum; 6FCT; -.
DR PDBsum; 6FCW; -.
DR PDBsum; 6FCY; -.
DR PDBsum; 6FD9; -.
DR PDBsum; 6FTT; -.
DR PDBsum; 6FU2; -.
DR PDBsum; 6FU7; -.
DR PDBsum; 6FUA; -.
DR PDBsum; 6R02; -.
DR PDBsum; 7Z6R; -.
DR PDBsum; 7Z8U; -.
DR AlphaFoldDB; Q4FQF7; -.
DR SMR; Q4FQF7; -.
DR STRING; 259536.Psyc_1903; -.
DR EnsemblBacteria; AAZ19751; AAZ19751; Psyc_1903.
DR KEGG; par:Psyc_1903; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_2_0_6; -.
DR OMA; YVMMDYD; -.
DR OrthoDB; 1419568at2; -.
DR BRENDA; 2.4.2.17; 13705.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000546; 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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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..231
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000229330"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:6FCC"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:6FCC"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:6FCC"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:6FCC"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:6FCC"
FT STRAND 104..122
FT /evidence="ECO:0007829|PDB:6FCC"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6FCY"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:6FCC"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:6FCC"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:6FCC"
FT STRAND 189..204
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6FCC"
FT HELIX 213..227
FT /evidence="ECO:0007829|PDB:6FCC"
SQ SEQUENCE 231 AA; 25156 MW; CEB30B859817130F CRC64;
MTEVTNSLPT SGLLNEANDE FLGLTLALSK GRILEETMPL LRAAGVELLE DPEASRKLIF
PTSNPNVRVL ILRASDVPTY VEHGAADFGV AGKDVLLEHG ANHVYELLDL KIAQCKLMTA
GVKDAPLPNR RLRIATKYVN VARAYFASQG QQVDVIKLYG SMELAPLVGL GDLIVDVVDT
GNTLRANGLE ARDHICDVSS RLIVNQVSYK RKFALLEPIL DSFKNSINST S
