ID G2Z1E0_FLABF Unreviewed; 199 AA.
AC G2Z1E0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=hisIE {ECO:0000256|HAMAP-Rule:MF_01019,
GN ECO:0000313|EMBL:CCB69708.1};
GN Synonyms=hisI {ECO:0000256|HAMAP-Rule:MF_01019};
GN OrderedLocusNames=FBFL15_1646 {ECO:0000313|EMBL:CCB69708.1};
OS Flavobacterium branchiophilum (strain FL-15).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1034807 {ECO:0000313|EMBL:CCB69708.1, ECO:0000313|Proteomes:UP000009186};
RN [1] {ECO:0000313|EMBL:CCB69708.1, ECO:0000313|Proteomes:UP000009186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FL-15 {ECO:0000313|EMBL:CCB69708.1,
RC ECO:0000313|Proteomes:UP000009186};
RX PubMed=21926215; DOI=10.1128/AEM.05625-11;
RG 1:IP;
RG Microbial Evolutionary Genomics,F-75015 Paris;
RG France 2:CNRS;
RG URA2171;
RG F-75015 Paris,France 3:Unite de Virologie et Immunologie Mol.;
RG INRA,78352 Jouy en Josas Cedex;
RG France. 4:Unite de Mathemathique;
RG Informatique et Genome,INRA;
RG 78352 Jouy en Josas Cedex;
RG France. 5:CEA/Genoscope;
RG Evry;
RG France;
RA Touchon M., Barbier P., Bernardet J.F., Loux V., Vacherie B., Barbe V.,
RA Rocha E.P., Duchaud E.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT branchiophilum.";
RL Appl. Environ. Microbiol. 77:7656-7662(2011).
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|HAMAP-Rule:MF_01019}.
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}.
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DR EMBL; FQ859183; CCB69708.1; -; Genomic_DNA.
DR RefSeq; WP_014084174.1; NC_016001.1.
DR AlphaFoldDB; G2Z1E0; -.
DR STRING; 1034807.FBFL15_1646; -.
DR KEGG; fbr:FBFL15_1646; -.
DR eggNOG; COG0139; Bacteria.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_048577_3_1_10; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000009186; Chromosome.
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; 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_01019; HisIE; 1.
DR InterPro; IPR023019; His_synth_HisIE.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
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; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
DR SUPFAM; SSF141734; HisI-like; 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}; Cytoplasm {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:UP000009186}.
FT DOMAIN 27..99
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000259|Pfam:PF01502"
FT REGION 1..109
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01019"
FT REGION 110..199
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01019"
SQ SEQUENCE 199 AA; 22499 MW; 6457D2C52A89BA5A CRC64;
MNINFSKSAH GLIPAIIQDS ETKAVLMLGY MNEEAFAKTQ EIKKVTFYSR SKQRLWTKGE
ESGNFLNLVS IKKDCDNDTL LIQVQPVGPT CHNGTDTCWA EENQPNYGFI STLEQTIKTR
RDNADAEKSY VASLFEKGIN KIAQKVGEEA VEVVIEAKDD NDDLFLSESA DLLFHYLILL
QAKGFQMNDV IEVLKKRQK
//