PUR9_HELMI
ID PUR9_HELMI Reviewed; 527 AA.
AC B0TEC5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=Helmi_29820;
GN ORFNames=HM1_3106;
OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliomicrobium.
OX NCBI_TaxID=498761;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51547 / Ice1;
RX PubMed=18441057; DOI=10.1128/jb.00299-08;
RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT of the Firmicutes containing the simplest photosynthetic apparatus.";
RL J. Bacteriol. 190:4687-4696(2008).
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}.
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DR EMBL; CP000930; ABZ85607.1; -; Genomic_DNA.
DR RefSeq; WP_012284078.1; NC_010337.2.
DR AlphaFoldDB; B0TEC5; -.
DR SMR; B0TEC5; -.
DR STRING; 498761.HM1_3106; -.
DR EnsemblBacteria; ABZ85607; ABZ85607; HM1_3106.
DR KEGG; hmo:HM1_3106; -.
DR eggNOG; COG0138; Bacteria.
DR HOGENOM; CLU_016316_5_2_9; -.
DR OMA; WRVAKFV; -.
DR OrthoDB; 1049662at2; -.
DR UniPathway; UPA00074; UER00133.
DR UniPathway; UPA00074; UER00135.
DR Proteomes; UP000008550; Chromosome.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
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 TIGRFAMs; TIGR00355; purH; 1.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Hydrolase; Multifunctional enzyme; Purine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..527
FT /note="Bifunctional purine biosynthesis protein PurH"
FT /id="PRO_1000096066"
FT DOMAIN 1..144
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
SQ SEQUENCE 527 AA; 56109 MW; E6823292C8E00394 CRC64;
MNRRALISVS DKTGVVDFAR GLADLGFEIV STGGTYQTIK AAGVPVTYVT EITGFPEILD
GRVKTLHPKV HGGILARRTP EHLAQLEAHA IVPIDVVAVN LYPFRETVAK PGVTREEAVE
NIDIGGPAMV RASAKNHESV AIIVNPDRYA TVLAELQQNG VVSEATRRAL AREAFAHTAE
YDAAIAAYLA AEAGDDDPFA GIFAPGKVEK VQDLRYGENP HQKAAFYRER GYRGAGAGTA
KQRWGKELSF NNLLDLNAAL ELVREFDRPA AAIIKHNNPC GVAVAATLKE AYEKAFAADP
VSAFGGIIAF NVAVDADTAN EVVKTFMEAV IAPSFDEAAL EILQQKKGLR IMETGPLADS
APATADVKKI RGGFLVQEAD LGDVTAEQIQ VVTERAPEEG ELADLLFAWK VVKHVKSNAI
VIAKDGVAIG VGAGQMNRVG SAQIALEQAK ASRAFGGDSV DHNNPAQGAV LASDAFLPFK
DTVETAARYG IRAIIQPGGS VRDAESIEAC NRLGVAMVFT GMRHFKH
