ID R5DJE8_9FIRM Unreviewed; 427 AA.
AC R5DJE8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Histidine biosynthesis bifunctional protein HisIE {ECO:0000256|HAMAP-Rule:MF_01019};
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_01019};
DE Short=PRA-CH {ECO:0000256|HAMAP-Rule:MF_01019};
DE EC=3.5.4.19 {ECO:0000256|HAMAP-Rule:MF_01019};
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000256|HAMAP-Rule:MF_01019};
DE Short=PRA-PH {ECO:0000256|HAMAP-Rule:MF_01019};
DE EC=3.6.1.31 {ECO:0000256|HAMAP-Rule:MF_01019};
GN Name=hisI {ECO:0000256|HAMAP-Rule:MF_01019};
GN Synonyms=hisIE {ECO:0000256|HAMAP-Rule:MF_01019};
GN ORFNames=BN457_00960 {ECO:0000313|EMBL:CCX76001.1};
OS Dorea sp. CAG:105.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=1262872 {ECO:0000313|EMBL:CCX76001.1, ECO:0000313|Proteomes:UP000017921};
RN [1] {ECO:0000313|EMBL:CCX76001.1, ECO:0000313|Proteomes:UP000017921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:105 {ECO:0000313|Proteomes:UP000017921};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC ChEBI:CHEBI:59457; EC=3.5.4.19;
CC Evidence={ECO:0000256|ARBA:ARBA00000024, ECO:0000256|HAMAP-
CC Rule:MF_01019};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00001460, ECO:0000256|HAMAP-
CC Rule:MF_01019};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC {ECO:0000256|ARBA:ARBA00005204, ECO:0000256|HAMAP-Rule:MF_01019}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC {ECO:0000256|ARBA:ARBA00005169, ECO:0000256|HAMAP-Rule:MF_01019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01019}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family.
CC {ECO:0000256|ARBA:ARBA00009667, ECO:0000256|RuleBase:RU003657}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC {ECO:0000256|ARBA:ARBA00007731, ECO:0000256|HAMAP-Rule:MF_01019}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
CC {ECO:0000256|ARBA:ARBA00008299, ECO:0000256|HAMAP-Rule:MF_01019}.
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:CCX76001.1}.
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DR EMBL; CAWY010000155; CCX76001.1; -; Genomic_DNA.
DR AlphaFoldDB; R5DJE8; -.
DR STRING; 1262872.BN457_00960; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000017921; 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:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.287.1080; MazG-like; 1.
DR Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 1.
DR HAMAP; MF_01020; HisE; 1.
DR HAMAP; MF_01021; HisI; 1.
DR HAMAP; MF_01019; HisIE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006062; His_biosynth.
DR InterPro; IPR023019; His_synth_HisIE.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR026660; PRA-CH.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR03188; histidine_hisI; 1.
DR PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR PANTHER; PTHR42945:SF1; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
DR SUPFAM; SSF141734; HisI-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01019};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01019};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01019};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW Rule:MF_01019};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01019};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_01019};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01019}; Reference proteome {ECO:0000313|Proteomes:UP000017921}.
FT DOMAIN 251..324
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
FT REGION 1..340
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01019"
FT REGION 341..427
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01019"
SQ SEQUENCE 427 AA; 48751 MW; 54816CF31CC7F998 CRC64;
MSYKRLIPCI FIAGGKAVKW FNDKSVLQDD VIALAKYYSD HGADELLVFD LSTSDDEHEE
AIDLMRRINR LIRIPMVAGG NIKRQEDVKK ILYAGAKRAM LNFSKPDSAK AVEEAAKRFG
KEKIAVSLND FDALFKHQHL IDEYSSEIVF MHRLDLNSVM DVTDIPCVIV TDTLEKPELF
KILKCPGVKG LSGKYVSQPD MDFVEFKKEC SEEGIQMTSF ESIMEFSQFK TNEQGLIPVI
VQHYKTREVL MLAYMNEESF DQTIKTGKMT YFSRSRQKLW VKGETSGHFQ YVKSLTIDCD
YDTLLAKVDQ VGAACHTGNP TCFFQHLAGT EYNEANPLEV FEIIYNTVVD RKENPKEGSY
TNYLFDKGID KILKKIGEEA TEIVIAAKNP SAEETKYEIS DFLYHMIVLM VEKGLNWEDI
VKELASR
//
