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Database: UniProt
Entry: A0A0G3HC91_9CORY
LinkDB: A0A0G3HC91_9CORY
Original site: A0A0G3HC91_9CORY 
ID   A0A0G3HC91_9CORY        Unreviewed;       281 AA.
AC   A0A0G3HC91;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|ARBA:ARBA00020998, ECO:0000256|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_00079};
DE            Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_00079};
DE            EC=2.4.2.17 {ECO:0000256|ARBA:ARBA00011946, ECO:0000256|HAMAP-Rule:MF_00079};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079,
GN   ECO:0000313|EMBL:AKK08772.1};
GN   ORFNames=CTEST_06670 {ECO:0000313|EMBL:AKK08772.1};
OS   Corynebacterium testudinoris.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08772.1, ECO:0000313|Proteomes:UP000035540};
RN   [1] {ECO:0000313|EMBL:AKK08772.1, ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK08772.1,
RC   ECO:0000313|Proteomes:UP000035540};
RX   PubMed=26227591;
RA   Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT   DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL   Genome Announc. 3:e00784-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000035540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT   recovered from necrotic lesions in the mouth of a tortoise.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024861, ECO:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000915, ECO:0000256|HAMAP-
CC         Rule:MF_00079};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00079};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by histidine.
CC       {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000256|ARBA:ARBA00004667, ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Long
CC       subfamily. {ECO:0000256|ARBA:ARBA00007955, ECO:0000256|HAMAP-
CC       Rule:MF_00079}.
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DR   EMBL; CP011545; AKK08772.1; -; Genomic_DNA.
DR   RefSeq; WP_047253073.1; NZ_JAASJB010000002.1.
DR   AlphaFoldDB; A0A0G3HC91; -.
DR   STRING; 136857.CTEST_06670; -.
DR   KEGG; cted:CTEST_06670; -.
DR   PATRIC; fig|136857.5.peg.1326; -.
DR   OrthoDB; 9801867at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000035540; 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   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   HAMAP; MF_00079; HisG_Long; 1.
DR   InterPro; IPR020621; ATP-PRT_HisG_long.
DR   InterPro; IPR013820; ATP_PRibTrfase_cat.
DR   InterPro; IPR018198; ATP_PRibTrfase_CS.
DR   InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR   InterPro; IPR013115; HisG_C.
DR   InterPro; IPR011322; N-reg_PII-like_a/b.
DR   InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C.
DR   NCBIfam; TIGR00070; hisG; 1.
DR   NCBIfam; TIGR03455; HisG_C-term; 1.
DR   PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR   Pfam; PF01634; HisG; 1.
DR   Pfam; PF08029; HisG_C; 1.
DR   SUPFAM; SSF54913; GlnB-like; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00079}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_00079};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_00079}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035540};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00079}.
FT   DOMAIN          49..190
FT                   /note="ATP phosphoribosyltransferase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01634"
FT   DOMAIN          206..276
FT                   /note="Histidine biosynthesis HisG C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08029"
SQ   SEQUENCE   281 AA;  30304 MW;  425BE1D477BDD615 CRC64;
     MIKIAVPNKG SLSEAAVEIL AEAGYKGRGD SKALAVFDTS NDVEFYFLRP KDIAIYVAAG
     MLDLGITGRD LARDSRAEVQ EVLSLGFGGS TFHYAGPADE EWRIEDLAGK RIATSYPNLV
     RDDLAARGID AEVIRLDGAV EISIKLGVAD AIADVVSTGN TLRRQGLATF GEPLVDSEAV
     IVSRAGTELT ADERVLLARI EGILHAQNYL MLDYNITRDR LDEVSRVTPG LSAPTVSPLA
     REDMVAVRAL VPRVRANDIM DELSQLGAQA ILATELRIVR I
//
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