HIS4_CAMJE
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 03-AUG-2022, entry version 117.
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 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; 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; NC_002163.1.
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; Q9PM74; -.
DR PRIDE; Q9PM74; -.
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 OMA; EWLHLVD; -.
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; -; 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 PANTHER; PTHR43090; PTHR43090; 1.
DR Pfam; PF00977; His_biosynth; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00007; TIGR00007; 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
