ID R6J038_9CLOT Unreviewed; 537 AA.
AC R6J038;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00125, ECO:0000256|HAMAP-Rule:MF_01018};
DE Includes:
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000256|HAMAP-Rule:MF_01018};
DE Short=ATP-PRT {ECO:0000256|HAMAP-Rule:MF_01018};
DE Short=ATP-PRTase {ECO:0000256|HAMAP-Rule:MF_01018};
DE EC=2.4.2.17 {ECO:0000256|HAMAP-Rule:MF_01018};
DE Includes:
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000256|HAMAP-Rule:MF_00125};
GN Name=hisG {ECO:0000256|HAMAP-Rule:MF_01018};
GN Synonyms=hisZ {ECO:0000256|HAMAP-Rule:MF_00125};
GN ORFNames=BN539_00906 {ECO:0000313|EMBL:CDB51006.1};
OS Clostridium sp. CAG:217.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262779 {ECO:0000313|EMBL:CDB51006.1, ECO:0000313|Proteomes:UP000018364};
RN [1] {ECO:0000313|EMBL:CDB51006.1, ECO:0000313|Proteomes:UP000018364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:217 {ECO:0000313|Proteomes:UP000018364};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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_01018}.
CC -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC allow the feedback regulation of ATP phosphoribosyltransferase activity
CC by histidine. {ECO:0000256|ARBA:ARBA00025246, ECO:0000256|HAMAP-
CC Rule:MF_00125}.
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_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:0000256|ARBA:ARBA00004667, ECO:0000256|HAMAP-Rule:MF_01018}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000256|HAMAP-Rule:MF_01018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01018}.
CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC HisZ. {ECO:0000256|HAMAP-Rule:MF_01018}.
CC -!- MISCELLANEOUS: This function is generally fulfilled by the C-terminal
CC part of HisG, which is missing in some bacteria such as this one.
CC {ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC subfamily. {ECO:0000256|ARBA:ARBA00009489, ECO:0000256|HAMAP-
CC Rule:MF_01018}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC HisZ subfamily. {ECO:0000256|ARBA:ARBA00005539, ECO:0000256|HAMAP-
CC Rule:MF_00125}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDB51006.1}.
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DR EMBL; CBDU010000015; CDB51006.1; -; Genomic_DNA.
DR AlphaFoldDB; R6J038; -.
DR STRING; 1262779.BN539_00906; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000018364; 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:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd13595; PBP2_HisGs; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR HAMAP; MF_01018; HisG_Short; 1.
DR HAMAP; MF_00125; HisZ; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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 InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004517; HisZ.
DR NCBIfam; TIGR00070; hisG; 1.
DR NCBIfam; TIGR00443; hisZ_biosyn_reg; 1.
DR PANTHER; PTHR21403:SF8; ATP PHOSPHORIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR21403; ATP PHOSPHORIBOSYLTRANSFERASE ATP-PRTASE; 1.
DR Pfam; PF01634; HisG; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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_01018};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01018};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01018};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01018};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_01018};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01018}; Reference proteome {ECO:0000313|Proteomes:UP000018364};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01018}.
FT DOMAIN 11..318
FT /note="Class II Histidinyl-tRNA synthetase (HisRS)-like
FT catalytic core"
FT /evidence="ECO:0000259|Pfam:PF13393"
FT DOMAIN 379..531
FT /note="ATP phosphoribosyltransferase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01634"
SQ SEQUENCE 537 AA; 59047 MW; 178D4CC17E9589B8 CRC64;
MKQYAKVTPE GSRDLLFEEC DDRRRVENAL TGLYEANGYR KVITPTLEFF DVFNSGDAGL
DADEMYKLTD NRGRTTVLRP DNTLPIARLV ATRLSEDAFP VRLYYNQSVF VRTKELAGRT
DEVAQSGIEL IGDGSMAADI QVITLACRAM QSTVPGFKIE LGHAGYFGAV LRNLNVKPAV
KAEICHLIEQ KNFAALGDLL DTLEDCRETR VLRRLPRLFG GPEVLDEARE LYTEGGADAS
LQYIKTLYDT LCAAGLQEQV LLDLGIVNRS NYYTGVIFRG YVQGSGLTVL SGGRYDNLLG
EFGTDKPAIG FAVDVSAVTD VLHEEINLDR PLRIALTKGR LEKASVQMFK TMGLNTEALE
NKGRRLILPV DPYEAVLSKA PDVITYVEHG VCDIGIVGKD TIVEHGSAFY EVLDLNIGRC
AFALATKKGT DFFSGYKRKT VASKYPKVAK EFFKSKGMDV DVIKIEGSVE LAPLLGLADG
IVDIVETGST LKENGLEVVE KIMPISARVI VNMASMKLRK DEIEAFLHDI ELAAQVG
//
