PUR9_THEMA
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 25-MAY-2022, entry version 141.
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}; OrderedLocusNames=TM_1249;
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-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:57454,
CC ChEBI:CHEBI:58467, ChEBI:CHEBI:58475; 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}.
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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.THEMA_08090; -.
DR EnsemblBacteria; AAD36324; AAD36324; TM_1249.
DR KEGG; tma:TM1249; -.
DR eggNOG; COG0138; Bacteria.
DR InParanoid; Q9X0X6; -.
DR OMA; WRVAKFV; -.
DR OrthoDB; 1049662at2; -.
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 Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 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; PTHR11692; 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; SSF52335; SSF52335; 1.
DR SUPFAM; SSF53927; SSF53927; 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
