HIS4_PAEAT
ID HIS4_PAEAT Reviewed; 247 AA.
AC A1R562;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, 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=AAur_1608;
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=290340;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1;
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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; CP000474; ABM09313.1; -; Genomic_DNA.
DR RefSeq; WP_011774319.1; NC_008711.1.
DR PDB; 4WD0; X-ray; 1.50 A; A=1-247.
DR PDBsum; 4WD0; -.
DR AlphaFoldDB; A1R562; -.
DR SMR; A1R562; -.
DR STRING; 290340.AAur_1608; -.
DR EnsemblBacteria; ABM09313; ABM09313; AAur_1608.
DR KEGG; aau:AAur_1608; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_11; -.
DR OMA; EWLHLVD; -.
DR OrthoDB; 794219at2; -.
DR UniPathway; UPA00031; UER00009.
DR Proteomes; UP000000637; 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:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:InterPro.
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; IPR010188; HisA/PriA_Actinobacteria.
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; TIGR01919; hisA-trpF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Isomerase; Reference proteome.
FT CHAIN 1..247
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000290447"
FT ACT_SITE 16
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT ACT_SITE 135
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01014"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:4WD0"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:4WD0"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:4WD0"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:4WD0"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:4WD0"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:4WD0"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:4WD0"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:4WD0"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 207..214
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:4WD0"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4WD0"
FT HELIX 237..244
FT /evidence="ECO:0007829|PDB:4WD0"
SQ SEQUENCE 247 AA; 26175 MW; A0839617E7505388 CRC64;
MTTSAQSVLE LLPAVDIVDG QAVRLLQGEA GSETSYGTPL EAALNWQNDG AEWVHMVDLD
AAFGRGNNAA LISDVVSQLN VKVELSGGLR DDESLERALE LGVARVNLGT AALENPEWTR
KAIDRFGDKI AVGLDVRGTT LAGRGWTKEG GDLWEVLARL EDAGCARYVV TDVTKDGTLQ
GPNVELLRQM VEKTGKPVVA SGGISSLEDL RVLRELVPLG VEGAIVGKAL YAGAFTLPEA
LDVAGRR
