ID   A0A2G5L8S2_9FLAO        Unreviewed;       285 AA.
AC   A0A2G5L8S2;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   05-DEC-2018, entry version 7.
DE   RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046302};
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|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046302};
GN   Name=hisG {ECO:0000256|HAMAP-Rule:MF_00079};
GN   ORFNames=BFP75_18105 {ECO:0000313|EMBL:PIB38121.1};
OS   Maribacter sp. 4G9.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1889777 {ECO:0000313|EMBL:PIB38121.1, ECO:0000313|Proteomes:UP000229780};
RN   [1] {ECO:0000313|EMBL:PIB38121.1, ECO:0000313|Proteomes:UP000229780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G9 {ECO:0000313|EMBL:PIB38121.1,
RC   ECO:0000313|Proteomes:UP000229780};
RA   Wong S.-K., Hamasaki K., Yoshizawa S.;
RT   "Draft genome of Maribacter sp. strain 4G9.";
RL   Submitted (AUG-2016) 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
CC       crucial role in the pathway because the rate of histidine
CC       biosynthesis seems to be controlled primarily by regulation of
CC       HisG enzymatic activity. {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + ATP;
CC         Xref=Rhea:RHEA:18473, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:58017, ChEBI:CHEBI:73183; EC=2.4.2.17;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00079,
CC         ECO:0000256|SAAS:SAAS00046298};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         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-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000256|HAMAP-Rule:MF_00079, ECO:0000256|SAAS:SAAS00046315}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family.
CC       Long subfamily. {ECO:0000256|HAMAP-Rule:MF_00079}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PIB38121.1}.
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; MDGL01000053; PIB38121.1; -; Genomic_DNA.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000229780; Unassembled WGS sequence.
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   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   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00046310};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Complete proteome {ECO:0000313|Proteomes:UP000229780};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00079};
KW   Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00021142, ECO:0000313|EMBL:PIB38121.1};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00046316};
KW   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:UP000229780};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00079,
KW   ECO:0000256|SAAS:SAAS00046311, ECO:0000313|EMBL:PIB38121.1}.
FT   DOMAIN       51    205       HisG. {ECO:0000259|Pfam:PF01634}.
FT   DOMAIN      210    282       HisG_C. {ECO:0000259|Pfam:PF08029}.
SQ   SEQUENCE   285 AA;  31484 MW;  EA8B6652503F5BDA CRC64;
     MTKIRIAIQK SGRLNEDSLQ ILKDCGISID NGKDQLKASS RNFPMEVFYL RNGDIPQYLR
     DGVVDVAIIG ENVLIEKGAD ISIAEKLGFS KCKVSLAVPK SVKYKSVEDF EGKRIATSYP
     NTVTNYLKEK GVNAELHIIN GSVEIAPNIG LADAICDIVS SGSTLFKNNL KEVEVMLTSE
     AVLAVSPQIS EERTALLKRL QFRIQSVLRA RKSKYVLLNA PNEKLQEILK LLPGMRSPTV
     LPLAEEGWSS VHTVIDKDTF WEVIDELKKA GAEGILVCPI EKMVL
//