(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BIJ2_GEOS0

ID   A0A0F6BIJ2_GEOS0        Unreviewed;       210 AA.
AC   A0A0F6BIJ2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 28.
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   OrderedLocusNames=GY4MC1_0402 {ECO:0000313|EMBL:ADP73243.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP73243.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP73243.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP73243.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-
CC         beta-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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01019, ECO:0000256|SAAS:SAAS01115149};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-
CC         beta-D-ribosyl)-5'-AMP + diphosphate + H(+);
CC         Xref=Rhea:RHEA:22828, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:59457, ChEBI:CHEBI:73183;
CC         EC=3.6.1.31; Evidence={ECO:0000256|HAMAP-Rule:MF_01019,
CC         ECO:0000256|SAAS:SAAS01118604};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01019, ECO:0000256|SAAS:SAAS00019969}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01019, ECO:0000256|SAAS:SAAS00976563}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01019,
CC       ECO:0000256|SAAS:SAAS00976539}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH
CC       family. {ECO:0000256|HAMAP-Rule:MF_01019,
CC       ECO:0000256|SAAS:SAAS00727852}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH
CC       family. {ECO:0000256|HAMAP-Rule:MF_01019,
CC       ECO:0000256|SAAS:SAAS00727862}.
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DR   EMBL; CP002293; ADP73243.1; -; Genomic_DNA.
DR   RefSeq; WP_013400006.1; NC_014650.1.
DR   EnsemblBacteria; ADP73243; ADP73243; GY4MC1_0402.
DR   KEGG; gmc:GY4MC1_0402; -.
DR   KO; K11755; -.
DR   OMA; VMACKDD; -.
DR   OrthoDB; 1842189at2; -.
DR   BioCyc; GSP581103:G1GOQ-447-MONOMER; -.
DR   UniPathway; UPA00031; UER00007.
DR   Proteomes; UP000002034; 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; 3.10.20.400; -; 1.
DR   HAMAP; MF_01020; HisE; 1.
DR   HAMAP; MF_01021; HisI; 1.
DR   HAMAP; MF_01019; HisIE; 1.
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   Pfam; PF01502; PRA-CH; 1.
DR   Pfam; PF01503; PRA-PH; 1.
DR   ProDom; PD002610; PRA_CycHdrlase; 1.
DR   SUPFAM; SSF141734; SSF141734; 1.
DR   TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BIJ2.
DR   SWISS-2DPAGE; A0A0F6BIJ2.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01019,
KW   ECO:0000256|SAAS:SAAS00976560};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01019,
KW   ECO:0000256|SAAS:SAAS00019974};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01019,
KW   ECO:0000256|SAAS:SAAS00976532};
KW   Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01019,
KW   ECO:0000256|SAAS:SAAS00976556};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01019,
KW   ECO:0000256|SAAS:SAAS00976548};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01019,
KW   ECO:0000256|SAAS:SAAS00976570};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01019,
KW   ECO:0000256|SAAS:SAAS00071035}.
FT   DOMAIN       28    101       PRA-CH. {ECO:0000259|Pfam:PF01502}.
FT   REGION        1    118       Phosphoribosyl-AMP cyclohydrolase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01019}.
FT   REGION      119    210       Phosphoribosyl-ATP pyrophosphohydrolase.
FT                                {ECO:0000256|HAMAP-Rule:MF_01019}.
SQ   SEQUENCE   210 AA;  23932 MW;  6949A8D5CC7D7A6D CRC64;
     MNLANIRFDE KGLVPAIVQD AQSKEVLMLA YMNEESLKKS LETGETWFYS RSRKELWHKG
     ATSGNIQRIV DMRYDCDSDS LLVLVEPAGP ACHTGSYSCF FNRMNGEKCE TSPNRFAILN
     TLEEIIAKRD AERPEGAYTT YLFEKGVDKI LKKVGEEAAE VIIAAKNRNH DELKWEVADL
     LYHLLVLLRE QKLPLDAVLE VLAERHNAKQ
//

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