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HIS2_PHOLL
ID   HIS2_PHOLL              Reviewed;         201 AA.
AC   Q7N6I6;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=plu1564;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(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         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; BX571864; CAE13857.1; -; Genomic_DNA.
DR   RefSeq; WP_011145861.1; NC_005126.1.
DR   AlphaFoldDB; Q7N6I6; -.
DR   SMR; Q7N6I6; -.
DR   STRING; 243265.plu1564; -.
DR   EnsemblBacteria; CAE13857; CAE13857; plu1564.
DR   GeneID; 24167061; -.
DR   KEGG; plu:plu1564; -.
DR   eggNOG; COG0139; Bacteria.
DR   eggNOG; COG0140; Bacteria.
DR   HOGENOM; CLU_048577_3_1_6; -.
DR   OMA; ERSCFHQ; -.
DR   OrthoDB; 1842189at2; -.
DR   BioCyc; PLUM243265:PLU_RS07880-MON; -.
DR   UniPathway; UPA00031; UER00007.
DR   UniPathway; UPA00031; UER00008.
DR   Proteomes; UP000002514; 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..201
FT                   /note="Histidine biosynthesis bifunctional protein HisIE"
FT                   /id="PRO_0000136421"
FT   REGION          1..114
FT                   /note="Phosphoribosyl-AMP cyclohydrolase"
FT   REGION          115..201
FT                   /note="Phosphoribosyl-ATP pyrophosphohydrolase"
SQ   SEQUENCE   201 AA;  22615 MW;  D6F71C699D6674BF CRC64;
     MLTAQQIEKL DWEKVAYMMP VIVQHAISGD VLMMGYMNKE ALNITISSGK ITFFSRSKQR
     LWTKGESSGH FLNLVNIYPD CDNDTLLALA DPIGPTCHFG THSCFAPAQT EWGFLYQLEK
     LLASRKTADP DHSYTAKLYA SGTKRIAQKV GEEGLETALA AAVNNREELT NEAADLMYHL
     MVLLQDQELD LSCVIRRLRE R
 
 
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