ID D3EF34_GEOS4 Unreviewed; 515 AA.
AC D3EF34;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Bifunctional purine biosynthesis protein PurH {ECO:0000256|HAMAP-Rule:MF_00139};
DE Includes:
DE RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_00139};
DE EC=2.1.2.3 {ECO:0000256|HAMAP-Rule:MF_00139};
DE AltName: Full=AICAR transformylase {ECO:0000256|HAMAP-Rule:MF_00139};
DE Includes:
DE RecName: Full=IMP cyclohydrolase {ECO:0000256|HAMAP-Rule:MF_00139};
DE EC=3.5.4.10 {ECO:0000256|HAMAP-Rule:MF_00139};
DE AltName: Full=ATIC {ECO:0000256|HAMAP-Rule:MF_00139};
DE AltName: Full=IMP synthase {ECO:0000256|HAMAP-Rule:MF_00139};
DE AltName: Full=Inosinicase {ECO:0000256|HAMAP-Rule:MF_00139};
GN Name=purH {ECO:0000256|HAMAP-Rule:MF_00139};
GN OrderedLocusNames=GYMC10_0947 {ECO:0000313|EMBL:ACX63245.1};
OS Geobacillus sp. (strain Y412MC10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=481743 {ECO:0000313|EMBL:ACX63245.1, ECO:0000313|Proteomes:UP000002381};
RN [1] {ECO:0000313|Proteomes:UP000002381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y412MC10 {ECO:0000313|Proteomes:UP000002381};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Brumm P., Mead D.;
RT "Complete sequence of Geobacillus sp. Y412MC10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACX63245.1, ECO:0000313|Proteomes:UP000002381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y412MC10 {ECO:0000313|EMBL:ACX63245.1,
RC ECO:0000313|Proteomes:UP000002381};
RX PubMed=23408395; DOI=10.4056/sigs.2605792;
RA Mead D.A., Lucas S., Copeland A., Lapidus A., Cheng J.F., Bruce D.C.,
RA Goodwin L.A., Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C.S.,
RA Tapia R., Land M., Hauser L.J., Chang Y.J., Kyrpides N.C., Ivanova N.N.,
RA Ovchinnikova G., Woyke T., Brumm C., Hochstein R., Schoenfeld T., Brumm P.;
RT "Complete Genome Sequence of Paenibacillus strain Y4.12MC10, a Novel
RT Paenibacillus lautus strain Isolated from Obsidian Hot Spring in
RT Yellowstone National Park.";
RL Stand. Genomic Sci. 6:381-400(2012).
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:0000256|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:0000256|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:0000256|ARBA:ARBA00004954, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00004844, ECO:0000256|HAMAP-Rule:MF_00139}.
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000256|HAMAP-Rule:MF_00139}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000256|ARBA:ARBA00007667,
CC ECO:0000256|HAMAP-Rule:MF_00139}.
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DR EMBL; CP001793; ACX63245.1; -; Genomic_DNA.
DR RefSeq; WP_012819099.1; NC_013406.1.
DR AlphaFoldDB; D3EF34; -.
DR STRING; 481743.GYMC10_0947; -.
DR KEGG; gym:GYMC10_0947; -.
DR HOGENOM; CLU_016316_5_2_9; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000002381; 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 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 NCBIfam; TIGR00355; purH; 1.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00139};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_00139};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_00139};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00139}.
FT DOMAIN 1..146
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 515 AA; 55554 MW; 9A6CE079B0DB1FB5 CRC64;
MGIKRALVSV SDKTGVVEFC RELSSLGVEI ISTGGTKNLL AKEGVPVIGI SDVTGFPEIL
DGRVKTLHPA VHSGLLAIRD SKEHQRQMQE LGLDYIDLVV VNLYPFQETI AKPDVEYEDA
IENIDIGGPT MLRSAAKNHA FVSVVVDAAD YGSVIEEIRG GGDTTLETRK RLAAKVFRHT
AAYDTLISDY LSNVTGDPLP ERFSVTYEKI QDLRYGENPH QKAAFYRKPL APAGTLTTAE
QLHGKELSYN NINDANAALQ IVKEFDEPTV VAVKHMNPCG VGIGTNVLEA YQKAYNADPT
SIFGGIVAAN RTIDAPTADL LKDIFLEIIL APDFTPEALE ILTKKKNIRL LKMGEFGSAK
ERQSTLAVTT IEGGMIVQES DVHSLDAADL KVVTDREPTE AELKQLLFGW KVVKHVKSNA
IILAADDMTV GVGAGQMNRV GSARIAVEQA GEKAKGAVLA SDAFFPMGDT VELAAKAGIT
AIIQPGGSIK DEESIKAANE YGIAMVFTGV RHFKH
//
