ID HIS2_XANAC Reviewed; 206 AA.
AC Q8PLG5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 16-JAN-2019, entry version 93.
DE RecName: Full=Histidine biosynthesis bifunctional protein HisIE {ECO:0000255|HAMAP-Rule:MF_01019};
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01019};
DE Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01019};
DE EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01019};
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_01019};
DE Short=PRA-PH {ECO:0000255|HAMAP-Rule:MF_01019};
DE EC=3.6.1.31 {ECO:0000255|HAMAP-Rule:MF_01019};
GN Name=hisI {ECO:0000255|HAMAP-Rule:MF_01019};
GN Synonyms=hisIE {ECO:0000255|HAMAP-Rule:MF_01019};
GN OrderedLocusNames=XAC1835;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A.,
RA Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C.,
RA Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F.,
RA Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R.,
RA El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C.,
RA Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A.,
RA Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F.,
RA Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M.,
RA Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H.,
RA Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R.,
RA Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F.,
RA Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D.,
RA Trindade dos Santos M., Truffi D., Tsai S.M., White F.F.,
RA Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing
RT host specificities.";
RL Nature 417:459-463(2002).
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:0000255|HAMAP-Rule:MF_01019};
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:0000255|HAMAP-
CC Rule:MF_01019};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC {ECO:0000255|HAMAP-Rule:MF_01019}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC {ECO:0000255|HAMAP-Rule:MF_01019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01019}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH
CC family. {ECO:0000255|HAMAP-Rule:MF_01019}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH
CC family. {ECO:0000255|HAMAP-Rule:MF_01019}.
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DR EMBL; AE008923; AAM36697.1; -; Genomic_DNA.
DR RefSeq; WP_003486226.1; NC_003919.1.
DR ProteinModelPortal; Q8PLG5; -.
DR SMR; Q8PLG5; -.
DR STRING; 190486.XAC1835; -.
DR EnsemblBacteria; AAM36697; AAM36697; XAC1835.
DR KEGG; xac:XAC1835; -.
DR eggNOG; ENOG4105K8F; Bacteria.
DR eggNOG; COG0139; LUCA.
DR eggNOG; COG0140; LUCA.
DR HOGENOM; HOG000277503; -.
DR KO; K11755; -.
DR OMA; VMACKDD; -.
DR BioCyc; XAXO190486:XAC_RS09330-MONOMER; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000000576; 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_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 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;
KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW Histidine biosynthesis; Hydrolase; Multifunctional enzyme;
KW Nucleotide-binding.
FT CHAIN 1 206 Histidine biosynthesis bifunctional
FT protein HisIE.
FT /FTId=PRO_0000136450.
FT REGION 1 117 Phosphoribosyl-AMP cyclohydrolase.
FT REGION 118 206 Phosphoribosyl-ATP pyrophosphohydrolase.
SQ SEQUENCE 206 AA; 22262 MW; 1B04984CEEFBD377 CRC64;
MGSNEVATGD PLATLDWNKG EGLLPVIVQD ADNLRVLMLG YMNAQALAVT QQRGEVTFFS
RSKQRLWTKG ESSGNVLRVV SIQTDCDADT LLVQARPHGP TCHLGRTSCF PSAPGQFLGS
LDALVAERER ERPHGSYTTK LFEQGIRRIA QKVGEEGVET ALAGVVQDDD ALLGESADLL
YHLIVLLRAR GLGLGDAAAL LESRHQ
//