PURE_TREDE
ID PURE_TREDE Reviewed; 159 AA.
AC Q73PV9;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Phosphoribosylaminoimidazole carboxylase {ECO:0000255|HAMAP-Rule:MF_02045, ECO:0000305};
DE EC=4.1.1.21 {ECO:0000255|HAMAP-Rule:MF_02045, ECO:0000269|PubMed:21548610};
DE AltName: Full=AIR carboxylase {ECO:0000255|HAMAP-Rule:MF_02045, ECO:0000303|PubMed:21548610};
DE Short=AIRC {ECO:0000255|HAMAP-Rule:MF_02045, ECO:0000305};
GN Name=purE {ECO:0000255|HAMAP-Rule:MF_02045, ECO:0000303|PubMed:21548610};
GN OrderedLocusNames=TDE_0687 {ECO:0000312|EMBL:AAS11180.1};
OS Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153
OS / KCTC 15104).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=15064399; DOI=10.1073/pnas.0307639101;
RA Seshadri R., Myers G.S.A., Tettelin H., Eisen J.A., Heidelberg J.F.,
RA Dodson R.J., Davidsen T.M., DeBoy R.T., Fouts D.E., Haft D.H., Selengut J.,
RA Ren Q., Brinkac L.M., Madupu R., Kolonay J.F., Durkin S.A., Daugherty S.C.,
RA Shetty J., Shvartsbeyn A., Gebregeorgis E., Geer K., Tsegaye G.,
RA Malek J.A., Ayodeji B., Shatsman S., McLeod M.P., Smajs D., Howell J.K.,
RA Pal S., Amin A., Vashisth P., McNeill T.Z., Xiang Q., Sodergren E.,
RA Baca E., Weinstock G.M., Norris S.J., Fraser C.M., Paulsen I.T.;
RT "Comparison of the genome of the oral pathogen Treponema denticola with
RT other spirochete genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:5646-5651(2004).
RN [2] {ECO:0007744|PDB:3RG8, ECO:0007744|PDB:3RGG}
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH 5-AMINOIMIDAZOLE
RP RIBONUCLEOTIDE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, MASS SPECTROMETRY, SUBFAMILY, AND MUTAGENESIS OF
RP HIS-40.
RC STRAIN=ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104;
RX PubMed=21548610; DOI=10.1021/bi102033a;
RA Tranchimand S., Starks C.M., Mathews I.I., Hockings S.C., Kappock T.J.;
RT "Treponema denticola PurE is a bacterial AIR carboxylase.";
RL Biochemistry 50:4623-4637(2011).
CC -!- FUNCTION: Catalyzes the reversible conversion of 5-aminoimidazole
CC ribonucleotide (AIR) and CO(2) to 4-carboxy-5-aminoimidazole
CC ribonucleotide (CAIR). Does not accept N5-carboxyaminoimidazole
CC ribonucleotide (N5-CAIR) as a substrate. {ECO:0000269|PubMed:21548610}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + H(+)
CC = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + CO2;
CC Xref=Rhea:RHEA:10792, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:77657, ChEBI:CHEBI:137981; EC=4.1.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02045,
CC ECO:0000269|PubMed:21548610};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 mM for CO(2) (at 10 degrees Celsius)
CC {ECO:0000269|PubMed:21548610};
CC KM=60 uM for AIR (at 10 degrees Celsius)
CC {ECO:0000269|PubMed:21548610};
CC Note=kcat is 77 sec(-1). {ECO:0000269|PubMed:21548610};
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole (carboxylase route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_02045, ECO:0000269|PubMed:21548610}.
CC -!- MASS SPECTROMETRY: Mass=17195; Mass_error=3; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:21548610};
CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class II subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02045, ECO:0000305|PubMed:21548610}.
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DR EMBL; AE017226; AAS11180.1; -; Genomic_DNA.
DR RefSeq; NP_971299.1; NC_002967.9.
DR RefSeq; WP_002681904.1; NC_002967.9.
DR PDB; 3RG8; X-ray; 1.74 A; A/B/C/D/E/F/G/H=1-159.
DR PDB; 3RGG; X-ray; 1.82 A; A/B/C/D=1-159.
DR PDB; 5C5D; X-ray; 1.69 A; A/B/C/D=1-159.
DR PDBsum; 3RG8; -.
DR PDBsum; 3RGG; -.
DR PDBsum; 5C5D; -.
DR AlphaFoldDB; Q73PV9; -.
DR SMR; Q73PV9; -.
DR STRING; 243275.TDE_0687; -.
DR EnsemblBacteria; AAS11180; AAS11180; TDE_0687.
DR GeneID; 2740246; -.
DR KEGG; tde:TDE_0687; -.
DR PATRIC; fig|243275.7.peg.667; -.
DR eggNOG; COG0041; Bacteria.
DR HOGENOM; CLU_094982_2_0_12; -.
DR OMA; TKPVIAC; -.
DR OrthoDB; 1560434at2; -.
DR BRENDA; 4.1.1.21; 6426.
DR UniPathway; UPA00074; UER00130.
DR EvolutionaryTrace; Q73PV9; -.
DR Proteomes; UP000008212; Chromosome.
DR GO; GO:0043727; F:5-amino-4-imidazole carboxylate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_02045; PurE_classII; 1.
DR InterPro; IPR033626; PurE_classII.
DR InterPro; IPR000031; PurE_dom.
DR InterPro; IPR024694; PurE_prokaryotes.
DR Pfam; PF00731; AIRC; 1.
DR PIRSF; PIRSF001338; AIR_carboxylase; 1.
DR SMART; SM01001; AIRC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Purine biosynthesis; Reference proteome.
FT CHAIN 1..159
FT /note="Phosphoribosylaminoimidazole carboxylase"
FT /id="PRO_0000434131"
FT BINDING 11
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045,
FT ECO:0000269|PubMed:21548610, ECO:0007744|PDB:3RGG"
FT BINDING 14
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045,
FT ECO:0000269|PubMed:21548610, ECO:0007744|PDB:3RGG"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045,
FT ECO:0000269|PubMed:21548610, ECO:0007744|PDB:3RGG"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045,
FT ECO:0000269|PubMed:21548610, ECO:0007744|PDB:3RGG"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045,
FT ECO:0000269|PubMed:21548610, ECO:0007744|PDB:3RGG"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02045,
FT ECO:0000269|PubMed:21548610, ECO:0007744|PDB:3RGG"
FT MUTAGEN 40
FT /note="H->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:21548610"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:5C5D"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:5C5D"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:5C5D"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:5C5D"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:5C5D"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:5C5D"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:5C5D"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:5C5D"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:5C5D"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5C5D"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5C5D"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:5C5D"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:5C5D"
FT HELIX 117..128
FT /evidence="ECO:0007829|PDB:5C5D"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:5C5D"
FT HELIX 133..157
FT /evidence="ECO:0007829|PDB:5C5D"
SQ SEQUENCE 159 AA; 17196 MW; F91B7B6D09DD8C87 CRC64;
MRPLVIILMG SSSDMGHAEK IASELKTFGI EYAIRIGSAH KTAEHVVSML KEYEALDRPK
LYITIAGRSN ALSGFVDGFV KGATIACPPP SDSFAGADIY SSLRMPSGIS PALVLEPKNA
ALLAARIFSL YDKEIADSVK SYMESNAQKI IEDDSKLKR
