HIS1_LACLA
ID HIS1_LACLA Reviewed; 208 AA.
AC Q02129; Q9CG94;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=ATP phosphoribosyltransferase;
DE Short=ATP-PRT;
DE Short=ATP-PRTase;
DE EC=2.4.2.17;
GN Name=hisG; OrderedLocusNames=LL1208; ORFNames=L0066;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 2118;
RX PubMed=1400209; DOI=10.1128/jb.174.20.6571-6579.1992;
RA Delorme C., Ehrlich S.D., Renault P.;
RT "Histidine biosynthesis genes in Lactococcus lactis subsp. lactis.";
RL J. Bacteriol. 174:6571-6579(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10430882; DOI=10.1073/pnas.96.16.8985;
RA Sissler M., Delorme C., Bond J., Ehrlich S.D., Renault P., Francklyn C.;
RT "An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:8985-8990(1999).
RN [4]
RP SUBUNIT.
RX PubMed=12269828; DOI=10.1021/bi020243z;
RA Bovee M.L., Champagne K.S., Demeler B., Francklyn C.S.;
RT "The quaternary structure of the HisZ-HisG N-1-(5'-phosphoribosyl)-ATP
RT transferase from Lactococcus lactis.";
RL Biochemistry 41:11838-11846(2002).
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 -!- 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: Heterooctamer composed of four HisG and four HisZ subunits.
CC {ECO:0000305|PubMed:12269828}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC HisZ.
CC -!- MISCELLANEOUS: The stability and homogeneity of the HisG-HisZ complex
CC is apparently increased by ATP and 5-phosphoribose 1-diphosphate but
CC decreased in the presence of the regulatory inhibitor histidine.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK05306.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U92974; AAB81903.1; -; Genomic_DNA.
DR EMBL; AE005176; AAK05306.1; ALT_FRAME; Genomic_DNA.
DR PIR; D45734; D45734.
DR PIR; H86775; H86775.
DR RefSeq; NP_267364.1; NC_002662.1.
DR PDB; 1Z7M; X-ray; 2.90 A; E/F/G/H=1-208.
DR PDB; 1Z7N; X-ray; 3.25 A; E/F/G/H=1-208.
DR PDBsum; 1Z7M; -.
DR PDBsum; 1Z7N; -.
DR AlphaFoldDB; Q02129; -.
DR SMR; Q02129; -.
DR STRING; 272623.L0066; -.
DR PaxDb; Q02129; -.
DR EnsemblBacteria; AAK05306; AAK05306; L0066.
DR KEGG; lla:L0066; -.
DR PATRIC; fig|272623.7.peg.1303; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_2_0_9; -.
DR BRENDA; 2.4.2.17; 2903.
DR UniPathway; UPA00031; UER00006.
DR EvolutionaryTrace; Q02129; -.
DR Proteomes; UP000002196; 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..208
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151911"
FT CONFLICT 51
FT /note="P -> A (in Ref. 1; AAB81903)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="Y -> D (in Ref. 1; AAB81903)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="H -> R (in Ref. 1; AAB81903)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 10..20
FT /evidence="ECO:0007829|PDB:1Z7M"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 51..59
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 70..75
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 143..146
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:1Z7M"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:1Z7M"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:1Z7M"
FT HELIX 185..202
FT /evidence="ECO:0007829|PDB:1Z7M"
SQ SEQUENCE 208 AA; 23677 MW; 8CE4CD0A16D39FEF CRC64;
MIKIAITKGR IQKQVTKLLE NADYDVEPIL NLGRELQIKT KDDLQIIFGK PNDVITFLEH
GIVDIGFVGK DTLDENDFDD YYELLYLKIG QCIFALASYP DFSNKNFQRH KRIASKYPRV
TKKYFAQKQE DIEIIKLEGS VELGPVVGLA DAIVDIVETG NTLSANGLEV IEKISDISTR
MIVNKSSFKF KKDKIIEMVE RLEDAQTN
