HIS4_THEMA
ID HIS4_THEMA Reviewed; 241 AA.
AC Q9X0C7;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 138.
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=TM_1037;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP ACTIVE SITES, SUBUNIT, AND MUTAGENESIS OF ASP-8; HIS-48; ASP-51; ARG-83;
RP ASP-127 AND THR-164.
RX PubMed=12356303; DOI=10.1021/bi026092h;
RA Henn-Sax M., Thoma R., Schmidt S., Hennig M., Kirschner K., Sterner R.;
RT "Two (betaalpha)(8)-barrel enzymes of histidine and tryptophan biosynthesis
RT have similar reaction mechanisms and common strategies for protecting their
RT labile substrates.";
RL Biochemistry 41:12032-12042(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=10968789; DOI=10.1126/science.289.5484.1546;
RA Lang D., Thoma R., Henn-Sax M., Sterner R., Wilmanns M.;
RT "Structural evidence for evolution of the beta/alpha barrel scaffold by
RT gene duplication and fusion.";
RL Science 289:1546-1550(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 -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12356303}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36114.1; -; Genomic_DNA.
DR PIR; D72304; D72304.
DR RefSeq; NP_228843.1; NC_000853.1.
DR RefSeq; WP_004080485.1; NZ_CP011107.1.
DR PDB; 1QO2; X-ray; 1.85 A; A/B=1-241.
DR PDB; 2CFF; X-ray; 2.50 A; A/B=1-241.
DR PDB; 2W79; X-ray; 1.85 A; A/B=1-241.
DR PDBsum; 1QO2; -.
DR PDBsum; 2CFF; -.
DR PDBsum; 2W79; -.
DR AlphaFoldDB; Q9X0C7; -.
DR SMR; Q9X0C7; -.
DR STRING; 243274.THEMA_09175; -.
DR PRIDE; Q9X0C7; -.
DR EnsemblBacteria; AAD36114; AAD36114; TM_1037.
DR KEGG; tma:TM1037; -.
DR eggNOG; COG0106; Bacteria.
DR InParanoid; Q9X0C7; -.
DR OMA; EWLHLVD; -.
DR OrthoDB; 794219at2; -.
DR SABIO-RK; Q9X0C7; -.
DR UniPathway; UPA00031; UER00009.
DR EvolutionaryTrace; Q9X0C7; -.
DR Proteomes; UP000008183; 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; -; 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..241
FT /note="1-(5-phosphoribosyl)-5-[(5-
FT phosphoribosylamino)methylideneamino] imidazole-4-
FT carboxamide isomerase"
FT /id="PRO_0000142068"
FT ACT_SITE 8
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:12356303"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:12356303"
FT MUTAGEN 8
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:12356303"
FT MUTAGEN 48
FT /note="H->A: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:12356303"
FT MUTAGEN 51
FT /note="D->N: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:12356303"
FT MUTAGEN 83
FT /note="R->N: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:12356303"
FT MUTAGEN 127
FT /note="D->N: Almost no activity."
FT /evidence="ECO:0000269|PubMed:12356303"
FT MUTAGEN 164
FT /note="T->A: Strong decrease in activity."
FT /evidence="ECO:0000269|PubMed:12356303"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1QO2"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:1QO2"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:1QO2"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:1QO2"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:1QO2"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:1QO2"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1QO2"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:2W79"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:1QO2"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1QO2"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 177..187
FT /evidence="ECO:0007829|PDB:1QO2"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:1QO2"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1QO2"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:1QO2"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:1QO2"
SQ SEQUENCE 241 AA; 27028 MW; B1ABDDE5A4D5213D CRC64;
MLVVPAIDLF RGKVARMIKG RKENTIFYEK DPVELVEKLI EEGFTLIHVV DLSNAIENSG
ENLPVLEKLS EFAEHIQIGG GIRSLDYAEK LRKLGYRRQI VSSKVLEDPS FLKSLREIDV
EPVFSLDTRG GRVAFKGWLA EEEIDPVSLL KRLKEYGLEE IVHTEIEKDG TLQEHDFSLT
KKIAIEAEVK VLAAGGISSE NSLKTAQKVH TETNGLLKGV IVGRAFLEGI LTVEVMKRYA
R
