HIS4_MYCLE
ID HIS4_MYCLE Reviewed; 244 AA.
AC Q9CC56; Q9X7C1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=ML1261; ORFNames=MLCB1610.24;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Involved in both the histidine and tryptophan biosynthetic
CC pathways. {ECO:0000250}.
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 -!- 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;
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAC31642.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL049913; CAB43170.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL583921; CAC31642.1; ALT_INIT; Genomic_DNA.
DR PIR; G87066; G87066.
DR PIR; T45250; T45250.
DR RefSeq; WP_010908231.1; NC_002677.1.
DR AlphaFoldDB; Q9CC56; -.
DR SMR; Q9CC56; -.
DR STRING; 272631.ML1261; -.
DR EnsemblBacteria; CAC31642; CAC31642; CAC31642.
DR KEGG; mle:ML1261; -.
DR Leproma; ML1261; -.
DR eggNOG; COG0106; Bacteria.
DR HOGENOM; CLU_048577_1_1_11; -.
DR OMA; EWLHLVD; -.
DR UniPathway; UPA00031; UER00009.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000000806; 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:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan 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; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Cytoplasm;
KW Histidine biosynthesis; Isomerase; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..244
FT /note="Phosphoribosyl isomerase A"
FT /id="PRO_0000142083"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 129
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 244 AA; 26003 MW; CABD3D38309800E8 CRC64;
MSLILLPAVD VVEGRAVRLV QGKAGSENDY GSALDAALCW QRDGADWIHL VDLDAAFGRG
SNRELLSEMV GKLDVQVELS GGIRDDDSLN AALATGCARV NLGTAACENP HWCAQVIAEH
GDKIAVGLDV QIVDGQHRLR GRGWETDGGD LWDVLENLDR QGCSRFIVTD VTKDGTLDGP
NLDLLASVSD RTNVPVIASG GVSSLDDLRA IAKFTERGIE GAIVGKALYA ERFTLPQALA
VVRM
