ID A0A1H9QJL3_9ACTN Unreviewed; 517 AA.
AC A0A1H9QJL3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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 ORFNames=SAMN05443377_103117 {ECO:0000313|EMBL:SER59953.1};
OS Propionibacterium cyclohexanicum.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=64702 {ECO:0000313|EMBL:SER59953.1, ECO:0000313|Proteomes:UP000198815};
RN [1] {ECO:0000313|EMBL:SER59953.1, ECO:0000313|Proteomes:UP000198815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16859 {ECO:0000313|EMBL:SER59953.1,
RC ECO:0000313|Proteomes:UP000198815};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOGZ01000003; SER59953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9QJL3; -.
DR STRING; 64702.SAMN05443377_103117; -.
DR OrthoDB; 9802065at2; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000198815; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000198815};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00139}.
FT DOMAIN 1..151
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 517 AA; 54787 MW; E30804BBD407A6F6 CRC64;
MSESTRKPIA RALVSVYDKT GLEELGRALA DAGVEIVSTG STAKRLAAAG VAVTPVEQLT
GFPECLDGRV KTLHPAIHAG LLADLRLDTH RKQLDELGIK PFDLVISNLY PFTETVASGA
EFDACIEQID IGGPSMVRAA AKNHPSVAIV TSTAQYALVE EALSKGGFTL EQRRTLAAQA
FAHTAAYDAA VASWLAEQTT SEGLPQFAGL AAHKVSDLRY GENSHQRAAV YALEGAAPGL
VGAQLLNGKA MSYNNYTDTD AARRAAYDYE RPAVAVIKHA NPCGIAVGAD IAEAHRKAHA
CDPLSAYGGV IAANRPVSLE MAQQVKPIFT EVIVAPGYDP DALELLRTKK NLRILLAEDY
RFEPSMWREI SGGLLVSDPD RLDAPGDDPA NWVLQAGPAA DEATLADLRF AWTACRSVKS
NAILLAHDGA SVGVGMGQVN RVDSCRLAVD RAGDRAKGSV AASDAYFPFS DGPQILMDAG
VRAIVEPGGS IRDEQTIAAA TQAGVTLYFT GNRHFFH
//
