ID R9ME94_9FIRM Unreviewed; 427 AA.
AC R9ME94;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=C818_02898 {ECO:0000313|EMBL:EOS69021.1};
OS Lachnospiraceae bacterium MD308.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1235799 {ECO:0000313|EMBL:EOS69021.1, ECO:0000313|Proteomes:UP000014117};
RN [1] {ECO:0000313|EMBL:EOS69021.1, ECO:0000313|Proteomes:UP000014117}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3-2 {ECO:0000313|EMBL:EOS69021.1,
RC ECO:0000313|Proteomes:UP000014117};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 3-2.";
RL Submitted (APR-2013) 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:EOS69021.1}.
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DR EMBL; ASTE01000037; EOS69021.1; -; Genomic_DNA.
DR AlphaFoldDB; R9ME94; -.
DR STRING; 1235799.C818_02898; -.
DR PATRIC; fig|1235799.3.peg.3044; -.
DR eggNOG; COG0107; Bacteria.
DR eggNOG; COG0139; Bacteria.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_048577_3_1_9; -.
DR OrthoDB; 9795769at2; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000014117; 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:UP000014117}.
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; 48839 MW; 1974C0B1C6B8F759 CRC64;
MSYKRLIPCI FIEGGKAVRW FHDDEVISED VVGLAKSYSD LGADELIIFD LSETDDEHEA
SIDLMRRINR VIRIPMIAGG NIRRQEDVKK ILYAGAKRAI INFSKYDGVE MMEEAKLRFG
KEKIAVSLND FDALFKRQRV IQECCSEIVF MHRLDLNSVM NVTDIPSVIV TDTMEEPELF
KILKCPGIKG LSGKYISQPE LDFKAFKEKC GIEGIKITSF ESIMDFSEFT LNGDGLIPVV
VQHYKTQEVL MLAYMNEEAF DCTIKTGKMT YYSRSRKTLW VKGETSGHFQ YVKSLTIDCD
KDTLLAKVDQ VGAACHTGNP TCFYQPLVGM NYDGKNPLQI FEMVYDTIVD RKEHPKEGSY
TNYLFDKGLD KILKKVGEEA TEIVIAAKNK NPEEIKYELA DFLYHAMVLM VEKDVKWEDI
IKELAER
//
