ID   HIS4_THEKO              Reviewed;         233 AA.
AC   Q5JFU9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 101.
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}; OrderedLocusNames=TK0247;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
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-beta-D-
CC         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-histidine
CC       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}.
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DR   EMBL; AP006878; BAD84436.1; -; Genomic_DNA.
DR   RefSeq; WP_011249202.1; NC_006624.1.
DR   AlphaFoldDB; Q5JFU9; -.
DR   SMR; Q5JFU9; -.
DR   STRING; 69014.TK0247; -.
DR   EnsemblBacteria; BAD84436; BAD84436; TK0247.
DR   GeneID; 78446751; -.
DR   KEGG; tko:TK0247; -.
DR   PATRIC; fig|69014.16.peg.246; -.
DR   eggNOG; arCOG00618; Archaea.
DR   HOGENOM; CLU_048577_1_2_2; -.
DR   InParanoid; Q5JFU9; -.
DR   OrthoDB; 52866at2157; -.
DR   PhylomeDB; Q5JFU9; -.
DR   UniPathway; UPA00031; UER00009.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IBA:GO_Central.
DR   GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR   CDD; cd04732; HisA; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_01014; HisA; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006062; His_biosynth.
DR   InterPro; IPR044524; Isoase_HisA-like.
DR   InterPro; IPR023016; Isoase_HisA-like_bact.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR43090; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   PANTHER; PTHR43090:SF7; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1.
DR   Pfam; PF00977; His_biosynth; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; Isomerase;
KW   Reference proteome.
FT   CHAIN           1..233
FT                   /note="1-(5-phosphoribosyl)-5-[(5-
FT                   phosphoribosylamino)methylideneamino] imidazole-4-
FT                   carboxamide isomerase"
FT                   /id="PRO_0000142102"
FT   ACT_SITE        8
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT   ACT_SITE        125
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
SQ   SEQUENCE   233 AA;  25886 MW;  4B7358F3C6E530AF CRC64;
     MEVYPAIDLM KGRAVRLYRG RRESVKVYGD PVKIAQGFSE LVDKIHVVDL DGAFEGRPRN
     LEVVERIIEE TGLRVQVGGG FRTYEAVGRA YEVGVENVIL GTKALDTAFL ERLTDEFGGI
     TVSLDVKDGR IAVKGWVEEG SIKVRDAFEI LRNYVNRFVY TSIERDGTLT GVDEIGRFWG
     DEEFIYAGGV SSAEDIVRLA ERGFSGVIVG KALYEGVVKL EDLLEVAKCL RRG
//