HIS2_SHIFL
ID HIS2_SHIFL Reviewed; 203 AA.
AC P37793;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Histidine biosynthesis bifunctional protein HisIE;
DE Includes:
DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase;
DE Short=PRA-CH;
DE EC=3.5.4.19;
DE Includes:
DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase;
DE Short=PRA-PH;
DE EC=3.6.1.31;
GN Name=hisI; Synonyms=hisIE; OrderedLocusNames=SF2088, S2209;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PE577 / Serotype 2a;
RX PubMed=7507920; DOI=10.1128/jb.176.3.733-747.1994;
RA Morona R., Mavris M., Fallarino A., Manning P.A.;
RT "Characterization of the rfc region of Shigella flexneri.";
RL J. Bacteriol. 176:733-747(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC {ECO:0000305}.
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DR EMBL; X71970; CAA50784.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN43628.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17456.1; -; Genomic_DNA.
DR RefSeq; NP_707921.1; NC_004337.2.
DR RefSeq; WP_000954863.1; NZ_WPGW01000112.1.
DR PDB; 6J22; X-ray; 2.20 A; A/B=2-203.
DR PDB; 6J2L; X-ray; 2.17 A; A/B=2-203.
DR PDBsum; 6J22; -.
DR PDBsum; 6J2L; -.
DR AlphaFoldDB; P37793; -.
DR SMR; P37793; -.
DR STRING; 198214.SF2088; -.
DR EnsemblBacteria; AAN43628; AAN43628; SF2088.
DR EnsemblBacteria; AAP17456; AAP17456; S2209.
DR GeneID; 1025295; -.
DR KEGG; sfl:SF2088; -.
DR KEGG; sfx:S2209; -.
DR PATRIC; fig|198214.7.peg.2497; -.
DR HOGENOM; CLU_048577_3_1_6; -.
DR OMA; ERSCFHQ; -.
DR UniPathway; UPA00031; UER00007.
DR UniPathway; UPA00031; UER00008.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Histidine biosynthesis; Hydrolase; Multifunctional enzyme;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..203
FT /note="Histidine biosynthesis bifunctional protein HisIE"
FT /id="PRO_0000136429"
FT REGION 1..114
FT /note="Phosphoribosyl-AMP cyclohydrolase"
FT REGION 115..203
FT /note="Phosphoribosyl-ATP pyrophosphohydrolase"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:6J2L"
FT TURN 12..17
FT /evidence="ECO:0007829|PDB:6J2L"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:6J2L"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:6J2L"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:6J2L"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:6J2L"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6J2L"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:6J2L"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6J2L"
FT TURN 64..68
FT /evidence="ECO:0007829|PDB:6J2L"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:6J2L"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:6J2L"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:6J2L"
FT TURN 104..107
FT /evidence="ECO:0007829|PDB:6J2L"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:6J2L"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6J22"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:6J2L"
FT HELIX 143..162
FT /evidence="ECO:0007829|PDB:6J2L"
FT HELIX 166..186
FT /evidence="ECO:0007829|PDB:6J2L"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:6J2L"
SQ SEQUENCE 203 AA; 22882 MW; 51EC7BDA1D0BAEC0 CRC64;
MLTEQQRREL DWEKTDGLMP VIVQHAVSGE VLMLGYMNPE ALDKTIESGK VTFFSRTKQR
LWIKGETSGN FLNVVSIAPD CDNDTLLVLA NPIGPTCHKG TSSCFGNTAH QWLFLYQLEQ
LLAERKYADP ETSYTAKLYA SGTKRIAQKV GEEGVETALA ATVHDRFELT NEASDLMYHL
LVLLQDQDLD LTTVIENLHK RHQ
