(data stored in ACNUC7421 zone)

SWISSPROT: HIS4_PSEPF

ID   HIS4_PSEPF              Reviewed;         245 AA.
AC   Q3KJI6;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase {ECO:0000255|HAMAP-Rule:MF_01014};
DE            EC=5.3.1.16 {ECO:0000255|HAMAP-Rule:MF_01014};
DE   AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase {ECO:0000255|HAMAP-Rule:MF_01014};
GN   Name=hisA {ECO:0000255|HAMAP-Rule:MF_01014};
GN   OrderedLocusNames=Pfl01_0326;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-
CC         ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-
CC         phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-
CC         beta-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469,
CC         ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01014};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-
CC       histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC       {ECO:0000255|HAMAP-Rule:MF_01014}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01014}.
CC   -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000255|HAMAP-
CC       Rule:MF_01014}.
DR   EMBL; CP000094; ABA72070.1; -; Genomic_DNA.
DR   RefSeq; WP_011332019.1; NC_007492.2.
DR   SMR; Q3KJI6; -.
DR   STRING; 205922.Pfl01_0326; -.
DR   PRIDE; Q3KJI6; -.
DR   EnsemblBacteria; ABA72070; ABA72070; Pfl01_0326.
DR   KEGG; pfo:Pfl01_0326; -.
DR   eggNOG; ENOG4105CJV; Bacteria.
DR   eggNOG; COG0106; LUCA.
DR   HOGENOM; HOG000224614; -.
DR   KO; K01814; -.
DR   OMA; EWLHLVD; -.
DR   BioCyc; PFLU205922:G1G4S-330-MONOMER; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04732; HisA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01014; HisA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR006063; HisA.
DR   InterPro; IPR023016; Isoase_HisA.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00007; TIGR00007; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJI6.
DR   SWISS-2DPAGE; Q3KJI6.
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm;
KW   Histidine biosynthesis; Isomerase.
FT   CHAIN         1    245       1-(5-phosphoribosyl)-5-[(5-
FT                                phosphoribosylamino)methylideneamino]
FT                                imidazole-4-carboxamide isomerase.
FT                                /FTId=PRO_0000229073.
FT   ACT_SITE      8      8       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01014}.
FT   ACT_SITE    130    130       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01014}.
SQ   SEQUENCE   245 AA;  25755 MW;  6FB13474D6BA6E86 CRC64;
     MLIIPAIDLK DGACVRLRQG RMEDSTVFSD DPVSMAAKWV EGGCRRLHLV DLNGAFEGQP
     VNGEVVTAIA KRYPTLPIQI GGGIRSLETI EHYVKAGVSY VIIGTKAVKD PAFVAEACRA
     FPGKIIVGLD AKDGFVATDG WAEISTVQVI DLAKQFEADG VSSIVYTDIA KDGMMQGCNV
     PFTAALAAAT KIPVIASGGI HNLGDIKSLL DAKVPGIIGA ITGRAIYEGT LDVAEAQAFC
     DSYQG
//

If you have problems or comments...

PBIL Back to PBIL home page