ID A0A1I2JLE1_9GAMM Unreviewed; 520 AA.
AC A0A1I2JLE1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN04488120_108115 {ECO:0000313|EMBL:SFF55662.1};
OS Fontimonas thermophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Fontimonas.
OX NCBI_TaxID=1076937 {ECO:0000313|EMBL:SFF55662.1, ECO:0000313|Proteomes:UP000199771};
RN [1] {ECO:0000313|EMBL:SFF55662.1, ECO:0000313|Proteomes:UP000199771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23609 {ECO:0000313|EMBL:SFF55662.1,
RC ECO:0000313|Proteomes:UP000199771};
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; FOOC01000008; SFF55662.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2JLE1; -.
DR STRING; 1076937.SAMN04488120_108115; -.
DR OrthoDB; 9802065at2; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000199771; 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:UP000199771};
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 520 AA; 55619 MW; D4AA79918C7ABC66 CRC64;
MKTPVRRALL SVSDKSGIVD FARALVERGV ALLSTGGTYK LLRDAGLPAA EVSQHTGFPE
IMDGRVKTLH PKIHGGLLGR RDIDAPVMQA HGIAPIDLLV VNLYPFEATV AKPDCTRAEA
IENIDIGGPA MLRAAAKNHA WVTVLTDPAD YAQVLAEIDA GGIKRHTRER LALKAFALTA
RYDAAVSAYL SSLQDDGTRT PFPGVLGLQF DKRQDLRYGE NPHQRAAFYV ERQPESGTIA
AARQLQGKEL SYNNIADADA ALECVKSFTA PACVIVKHAN PCGVAVRATI REAYEDAFRT
DPTSAFGGII AFNRELDGDT AKLIVERQFV EVIVAPQISA AARAAVAAKH NVRLLECGAF
PAQRATAWDF KRVAGGLLVQ DIDALDIGDG GLRVVTRRAP TPAELRDLRF AWQVAKFVKS
NAIVYAKNQM TIGIGAGQMS RVYSAKIAGI KAADEKLEVS GSVMASDAFF PFRDGIDAAA
AAGITAVIQP GGSLRDAEVI AAADEAGMAM VFTGVRHFRH
//
