ID HIS4_CAMJE Reviewed; 243 AA. AC Q9PM74; Q0P827; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; DE EC=5.3.1.16; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; GN Name=hisA; OrderedLocusNames=Cj1601; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). 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 -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL111168; CAL35698.1; -; Genomic_DNA. DR PIR; G81255; G81255. DR RefSeq; WP_002851391.1; NZ_SZUC01000002.1. DR RefSeq; YP_002344970.1; NC_002163.1. DR PDB; 4GJ1; X-ray; 2.15 A; A=1-243. DR PDBsum; 4GJ1; -. DR AlphaFoldDB; Q9PM74; -. DR SMR; Q9PM74; -. DR STRING; 192222.Cj1601; -. DR PaxDb; 192222-Cj1601; -. DR EnsemblBacteria; CAL35698; CAL35698; Cj1601. DR GeneID; 904505; -. DR KEGG; cje:Cj1601; -. DR PATRIC; fig|192222.6.peg.1577; -. DR eggNOG; COG0106; Bacteria. DR HOGENOM; CLU_048577_1_2_7; -. DR OrthoDB; 9807749at2; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000799; 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; Aldolase class I; 1. DR HAMAP; MF_01014; HisA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR006063; HisA_bact_arch. DR InterPro; IPR044524; Isoase_HisA-like. DR InterPro; IPR023016; Isoase_HisA-like_bact. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR NCBIfam; TIGR00007; 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase; 1. DR PANTHER; PTHR43090; 1-(5-PHOSPHORIBOSYL)-5-[(5-PHOSPHORIBOSYLAMINO)METHYLIDENEAMINO] IMIDAZOLE-4-CARBOXAMIDE ISOMERASE; 1. DR PANTHER; PTHR43090:SF2; 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 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis; KW Isomerase; Reference proteome. FT CHAIN 1..243 FT /note="1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] imidazole-4- FT carboxamide isomerase" FT /id="PRO_0000141993" FT ACT_SITE 9 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 131 FT /note="Proton donor" FT /evidence="ECO:0000250" FT STRAND 3..11 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 14..19 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 21..23 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 33..43 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 47..52 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 53..57 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 64..73 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 76..83 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 87..95 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 99..103 FT /evidence="ECO:0007829|PDB:4GJ1" FT TURN 105..109 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 111..121 FT /evidence="ECO:0007829|PDB:4GJ1" FT TURN 123..125 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 126..140 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 153..161 FT /evidence="ECO:0007829|PDB:4GJ1" FT TURN 162..164 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 167..172 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 184..193 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 208..213 FT /evidence="ECO:0007829|PDB:4GJ1" FT TURN 214..217 FT /evidence="ECO:0007829|PDB:4GJ1" FT STRAND 219..223 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 225..228 FT /evidence="ECO:0007829|PDB:4GJ1" FT HELIX 234..241 FT /evidence="ECO:0007829|PDB:4GJ1" SQ SEQUENCE 243 AA; 26684 MW; 23AE7D77A2ECD9A9 CRC64; MTQIIPALDL IDGEVVRLVK GDYEQKKVYK YNPLKKFKEY EKAGAKELHL VDLTGAKDPS KRQFALIEKL AKEVSVNLQV GGGIRSKEEV KALLDCGVKR VVIGSMAIKD ATLCLEILKE FGSEAIVLAL DTILKEDYVV AVNAWQEASD KKLMEVLDFY SNKGLKHILC TDISKDGTMQ GVNVRLYKLI HEIFPNICIQ ASGGVASLKD LENLKGICSG VIVGKALLDG VFSVEEGIRC LAN //