ID PUR9_THEMA Reviewed; 452 AA. AC Q9X0X6; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 148. DE RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000255|HAMAP-Rule:MF_00139}; DE Includes: DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_00139}; DE EC=2.1.2.3 {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=AICAR transformylase {ECO:0000255|HAMAP-Rule:MF_00139}; DE Includes: DE RecName: Full=IMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_00139}; DE EC=3.5.4.10 {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=ATIC {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=IMP synthase {ECO:0000255|HAMAP-Rule:MF_00139}; DE AltName: Full=Inosinicase {ECO:0000255|HAMAP-Rule:MF_00139}; GN Name=purH {ECO:0000255|HAMAP-Rule:MF_00139}; GN OrderedLocusNames=TM_1249; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC 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). CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D- CC ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide; CC Xref=Rhea:RHEA:22192, ChEBI:CHEBI:57453, ChEBI:CHEBI:58467, CC ChEBI:CHEBI:58475, ChEBI:CHEBI:195366; EC=2.1.2.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + IMP = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide; Xref=Rhea:RHEA:18445, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:58467; EC=3.5.4.10; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00139}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5- CC formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino- CC 1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): CC step 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; IMP CC from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal CC region. {ECO:0000255|HAMAP-Rule:MF_00139}. CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000255|HAMAP- CC Rule:MF_00139, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000512; AAD36324.1; -; Genomic_DNA. DR PIR; C72277; C72277. DR RefSeq; NP_229054.1; NC_000853.1. DR RefSeq; WP_004080014.1; NZ_CP011107.1. DR PDB; 1ZCZ; X-ray; 1.88 A; A/B=1-452. DR PDBsum; 1ZCZ; -. DR AlphaFoldDB; Q9X0X6; -. DR SMR; Q9X0X6; -. DR STRING; 243274.TM_1249; -. DR PaxDb; 243274-THEMA_08090; -. DR EnsemblBacteria; AAD36324; AAD36324; TM_1249. DR KEGG; tma:TM1249; -. DR eggNOG; COG0138; Bacteria. DR InParanoid; Q9X0X6; -. DR OrthoDB; 9802065at2; -. DR BRENDA; 3.5.4.10; 6331. DR UniPathway; UPA00074; UER00133. DR UniPathway; UPA00074; UER00135. DR EvolutionaryTrace; Q9X0X6; -. DR Proteomes; UP000008183; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IBA:GO_Central. DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central. DR CDD; cd01421; IMPCH; 1. DR Gene3D; 3.40.140.20; -; 2. DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1. DR HAMAP; MF_00139; PurH; 1. DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR036914; MGS-like_dom_sf. DR InterPro; IPR002695; PurH-like. DR PANTHER; PTHR11692:SF0; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC; 1. DR PANTHER; PTHR11692; BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH; 1. DR Pfam; PF01808; AICARFT_IMPCHas; 1. DR Pfam; PF02142; MGS; 1. DR PIRSF; PIRSF000414; AICARFT_IMPCHas; 1. DR SMART; SM00798; AICARFT_IMPCHas; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF53927; Cytidine deaminase-like; 1. DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1. DR PROSITE; PS51855; MGS; 1. PE 1: Evidence at protein level; KW 3D-structure; Hydrolase; Multifunctional enzyme; Purine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1..452 FT /note="Bifunctional purine biosynthesis protein PurH" FT /id="PRO_0000192142" FT DOMAIN 1..115 FT /note="MGS-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202" FT STRAND 3..7 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 15..23 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 32..40 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 48..51 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:1ZCZ" FT TURN 61..64 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 67..74 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 75..77 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 96..106 FT /evidence="ECO:0007829|PDB:1ZCZ" FT TURN 107..110 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 117..125 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 129..154 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 158..165 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 179..183 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 186..190 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 198..212 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 215..223 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 226..232 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 236..246 FT /evidence="ECO:0007829|PDB:1ZCZ" FT TURN 247..253 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 254..260 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 264..269 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 274..278 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 284..290 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 296..300 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 306..311 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 314..319 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 328..332 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 337..352 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 358..362 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 365..370 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 376..387 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 388..391 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 395..400 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 405..413 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 418..421 FT /evidence="ECO:0007829|PDB:1ZCZ" FT HELIX 428..438 FT /evidence="ECO:0007829|PDB:1ZCZ" FT STRAND 441..444 FT /evidence="ECO:0007829|PDB:1ZCZ" SQ SEQUENCE 452 AA; 49867 MW; E4537EF51A5C4469 CRC64; MKRILVSLYE KEKYLDILRE LHEKGWEIWA SSGTAKFLKS NGIEANDVST ITGFENLLGG LVKTLHPEIF AGILGPEPRW DVVFVDLYPP PDIDIGGVAL LRAAAKNWKK VKPAFDMETL KLAIEIDDEE TRKYLAGMTF AFTSVYDSIR ANQFVEGISL AFKREDLQLR YGENPHEKAF VYGKPAFEIL HEGKTISFNN ILDAENAWFM AKNLPRMGAV VVKHQSPCGA AIGEDKVEIV KKAIEADDES SFGGILAVNF EMDEEVAKSL KKYLEVIVAP SFTQEAIEVL SKKKVRLLKP GDYASWAGKM AFGSLVLSER KYPEGNFELV VGEPLSEKEL EDLEFAYRVV EGAKSNAVLI AKDGVTVGIG SGQPSRKRAA WIATVMAGEK AKGAVAASDA FFPFPDSLEI LAQAGVKAVV APLGSIRDEE VIEKARELGI TFYKAPSRVF RH //