HIS2_XANCP
ID HIS2_XANCP Reviewed; 206 AA.
AC Q8P9N8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=XCC1815;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
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., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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:0000255|HAMAP-Rule:MF_01019};
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; Evidence={ECO:0000255|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:0000255|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: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 family.
CC {ECO:0000255|HAMAP-Rule:MF_01019}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC {ECO:0000255|HAMAP-Rule:MF_01019}.
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DR EMBL; AE008922; AAM41104.1; -; Genomic_DNA.
DR RefSeq; NP_637180.1; NC_003902.1.
DR RefSeq; WP_011036985.1; NC_003902.1.
DR AlphaFoldDB; Q8P9N8; -.
DR SMR; Q8P9N8; -.
DR STRING; 340.xcc-b100_2102; -.
DR EnsemblBacteria; AAM41104; AAM41104; XCC1815.
DR KEGG; xcc:XCC1815; -.
DR PATRIC; fig|190485.4.peg.1935; -.
DR eggNOG; COG0139; Bacteria.
DR eggNOG; COG0140; Bacteria.
DR HOGENOM; CLU_048577_3_1_6; -.
DR OMA; ERSCFHQ; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000001010; 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; 3.10.20.810; -; 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 SUPFAM; SSF141734; SSF141734; 1.
DR TIGRFAMs; TIGR03188; histidine_hisI; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Histidine biosynthesis;
KW Hydrolase; Multifunctional enzyme; Nucleotide-binding; Reference proteome.
FT CHAIN 1..206
FT /note="Histidine biosynthesis bifunctional protein HisIE"
FT /id="PRO_0000136451"
FT REGION 1..117
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 118..206
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
SQ SEQUENCE 206 AA; 22175 MW; 121D52530770B61C CRC64;
MGSETTAAGD ALDALDWNKG DGLLPVIVQD ADNLRVLMLG YMNAEALAVT RARGEVTFFS
RSKQRLWTKG ESSGNVLRVV AIETDCDADT LLVQARPHGP TCHLGRTSCF PTAPSQFLGS
LDALIAEREH ERPHGSYTTK LFEQGIRRIA QKVGEEGVET ALAGVVQGDA ELLGESADLL
YHLIVLLRAR GLGLGDAVAL LESRHK
