HIS4_STRCO
ID HIS4_STRCO Reviewed; 240 AA.
AC P16250;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Phosphoribosyl isomerase A;
DE AltName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase;
DE EC=5.3.1.16;
DE AltName: Full=N-(5'-phosphoribosyl)anthranilate isomerase;
DE Short=PRAI;
DE EC=5.3.1.24;
DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase;
GN Name=priA; Synonyms=hisA; OrderedLocusNames=SCO2050; ORFNames=SC4G6.19c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RX PubMed=2199329; DOI=10.1016/0378-1119(90)90436-u;
RA Limauro D., Avitabile A., Cappellano M., Puglia A.M., Bruni C.B.;
RT "Cloning and characterization of the histidine biosynthetic gene cluster of
RT Streptomyces coelicolor A3(2).";
RL Gene 90:31-41(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP INVOLVEMENT IN HISTIDINE AND TRYPTOPHAN BIOSYNTHESIS.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12634849; DOI=10.1038/sj.embor.embor771;
RA Barona-Gomez F., Hodgson D.A.;
RT "Occurrence of a putative ancient-like isomerase involved in histidine and
RT tryptophan biosynthesis.";
RL EMBO Rep. 4:296-300(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=15654319; DOI=10.1038/sj.embor.7400330;
RA Kuper J., Doenges C., Wilmanns M.;
RT "Two-fold repeated (beta alpha)4 half-barrels may provide a molecular tool
RT for dual substrate specificity.";
RL EMBO Rep. 6:134-139(2005).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MUTAGENESIS OF ASP-11; ARG-19;
RP SER-81; ASP-130; THR-166 AND ASP-171.
RX PubMed=17967415; DOI=10.1016/j.bbrc.2007.10.101;
RA Wright H., Noda-Garcia L., Ochoa-Leyva A., Hodgson D.A., Fueloep V.,
RA Barona-Gomez F.;
RT "The structure/function relationship of a dual-substrate (beta alpha)8-
RT isomerase.";
RL Biochem. Biophys. Res. Commun. 365:16-21(2008).
CC -!- FUNCTION: Catalyzes the isomerization of the aminoaldose moiety of
CC ProFAR to the aminoketose of PRFAR in the biosynthesis pathway for
CC histidine and the isomerization of the aminoaldose PRA to the
CC aminoketose CdRP in the biosynthsis pathway for tryptophan.
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:0000269|PubMed:15654319};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC EC=5.3.1.24; Evidence={ECO:0000269|PubMed:15654319};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=28 uM for ProFAR {ECO:0000269|PubMed:15654319};
CC KM=4 uM for PRA {ECO:0000269|PubMed:15654319};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15654319}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
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DR EMBL; M31628; AAA26760.1; -; Genomic_DNA.
DR EMBL; AL939111; CAB51442.1; -; Genomic_DNA.
DR PIR; JQ0641; JQ0641.
DR RefSeq; NP_626310.1; NC_003888.3.
DR RefSeq; WP_003976766.1; NZ_VNID01000001.1.
DR PDB; 1VZW; X-ray; 1.80 A; A=1-240.
DR PDB; 2VEP; X-ray; 1.80 A; A=1-240.
DR PDB; 2X30; X-ray; 1.95 A; A=1-240.
DR PDB; 5DN1; X-ray; 1.95 A; A=1-240.
DR PDBsum; 1VZW; -.
DR PDBsum; 2VEP; -.
DR PDBsum; 2X30; -.
DR PDBsum; 5DN1; -.
DR AlphaFoldDB; P16250; -.
DR SMR; P16250; -.
DR STRING; 100226.SCO2050; -.
DR GeneID; 1097484; -.
DR KEGG; sco:SCO2050; -.
DR PATRIC; fig|100226.15.peg.2081; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_11; -.
DR InParanoid; P16250; -.
DR OMA; EWLHLVD; -.
DR PhylomeDB; P16250; -.
DR BRENDA; 5.3.1.24; 5998.
DR SABIO-RK; P16250; -.
DR UniPathway; UPA00031; UER00009.
DR UniPathway; UPA00035; UER00042.
DR EvolutionaryTrace; P16250; -.
DR Proteomes; UP000001973; 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:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
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; 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; Aromatic amino acid biosynthesis;
KW Cytoplasm; Histidine biosynthesis; Isomerase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..240
FT /note="Phosphoribosyl isomerase A"
FT /id="PRO_0000142087"
FT ACT_SITE 11
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 130
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT MUTAGEN 11
FT /note="D->A: No activity."
FT /evidence="ECO:0000269|PubMed:17967415"
FT MUTAGEN 19
FT /note="R->A: No effect on activity toward PRA. No activity
FT toward ProFAR."
FT /evidence="ECO:0000269|PubMed:17967415"
FT MUTAGEN 81
FT /note="S->T: No activity toward PRA. Almost no effect on
FT activity toward ProFAR."
FT /evidence="ECO:0000269|PubMed:17967415"
FT MUTAGEN 130
FT /note="D->A: Very low activity toward PRA. No activity
FT toward ProFAR."
FT /evidence="ECO:0000269|PubMed:17967415"
FT MUTAGEN 130
FT /note="D->Q: No activity."
FT /evidence="ECO:0000269|PubMed:17967415"
FT MUTAGEN 166
FT /note="T->A: No activity."
FT /evidence="ECO:0000269|PubMed:17967415"
FT MUTAGEN 171
FT /note="D->A: Low activity toward PRA. No activity toward
FT ProFAR."
FT /evidence="ECO:0000269|PubMed:17967415"
FT STRAND 5..13
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2X30"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 87..95
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:5DN1"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:5DN1"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:2VEP"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:2VEP"
FT HELIX 179..187
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:1VZW"
FT TURN 210..215
FT /evidence="ECO:0007829|PDB:1VZW"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:1VZW"
FT HELIX 232..239
FT /evidence="ECO:0007829|PDB:1VZW"
SQ SEQUENCE 240 AA; 25080 MW; A150E831DDABC76F CRC64;
MSKLELLPAV DVRDGQAVRL VHGESGTETS YGSPLEAALA WQRSGAEWLH LVDLDAAFGT
GDNRALIAEV AQAMDIKVEL SGGIRDDDTL AAALATGCTR VNLGTAALET PEWVAKVIAE
HGDKIAVGLD VRGTTLRGRG WTRDGGDLYE TLDRLNKEGC ARYVVTDIAK DGTLQGPNLE
LLKNVCAATD RPVVASGGVS SLDDLRAIAG LVPAGVEGAI VGKALYAKAF TLEEALEATS
