ID A0A168I679_9ACTN Unreviewed; 818 AA.
AC A0A168I679;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=purN {ECO:0000256|HAMAP-Rule:MF_01930};
GN Synonyms=purH {ECO:0000256|HAMAP-Rule:MF_00139};
GN ORFNames=UG55_109919 {ECO:0000313|EMBL:OAA18816.1};
OS Frankia sp. EI5c.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=683316 {ECO:0000313|EMBL:OAA18816.1, ECO:0000313|Proteomes:UP000077018};
RN [1] {ECO:0000313|EMBL:OAA18816.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA18816.1,
RC ECO:0000313|Proteomes:UP000077018};
RX PubMed=27389275;
RA D'Angelo T., Oshone R., Abebe-Akele F., Simpson S., Morris K., Thomas W.K.,
RA Tisa L.S.;
RT "Permanent Draft Genome Sequence for Frankia sp. Strain EI5c, a Single-
RT Spore Isolate of a Nitrogen-Fixing Actinobacterium, Isolated from the Root
RT Nodules of Elaeagnus angustifolia.";
RL Genome Announc. 4:e00660-16(2016).
RN [2] {ECO:0000313|EMBL:OAA18816.1, ECO:0000313|Proteomes:UP000077018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EI5c {ECO:0000313|EMBL:OAA18816.1,
RC ECO:0000313|Proteomes:UP000077018};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a formyl group from 10-
CC formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR),
CC producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and
CC tetrahydrofolate. {ECO:0000256|HAMAP-Rule:MF_01930}.
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=(6R)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-
CC formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide;
CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366;
CC EC=2.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01930};
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 -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC ribosyl)glycinamide (10-formyl THF route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005054, ECO:0000256|HAMAP-Rule:MF_01930}.
CC -!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
CC region. {ECO:0000256|HAMAP-Rule:MF_00139}.
CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000256|HAMAP-
CC Rule:MF_01930}.
CC -!- SIMILARITY: Belongs to the PurH family. {ECO:0000256|ARBA:ARBA00007667,
CC ECO:0000256|HAMAP-Rule:MF_00139}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01930}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAA18816.1}.
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DR EMBL; LRTK01000099; OAA18816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168I679; -.
DR STRING; 683316.UG55_109919; -.
DR PATRIC; fig|683316.3.peg.5413; -.
DR OrthoDB; 9802065at2; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000077018; 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:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd08645; FMT_core_GART; 1.
DR CDD; cd01421; IMPCH; 1.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_00139; PurH; 1.
DR HAMAP; MF_01930; PurN; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR004607; GART.
DR InterPro; IPR001555; GART_AS.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR002695; PurH-like.
DR NCBIfam; TIGR00355; purH; 1.
DR NCBIfam; TIGR00639; PurN; 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; PF00551; Formyl_trans_N; 1.
DR Pfam; PF02142; MGS; 1.
DR SMART; SM00798; AICARFT_IMPCHas; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR PROSITE; PS00373; GART; 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:UP000077018};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00139}.
FT DOMAIN 293..445
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 194..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 66
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 91..94
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 106
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT SITE 144
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
SQ SEQUENCE 818 AA; 84190 MW; 58DEC2521E01EC14 CRC64;
MPARLVVLAS GAGTTLQAIL DACADQAFGA RVAAVGTDRA DTLAQRRAEA VGVPVFTVRL
EDFADRAAFN EATAGRIAEY DPDLLVLAGY MKILGPQVIS RFPTVNTHPS LLPAFPGAHA
VRDALAAGVP TSGVTVHWVD EGVDTGPVIA QAPVPVQSDD DEDALRARIQ AVERGLFVSV
IGRYVRGELS WEGGRRGTTA ADADDVDAPV PGGARPEAGR TSPSPGGATG RGGGTDQAVE
AHANGGIVEG SGGIVSGASA VSGASGASAT ETGQGVPGGA AATDGSPQTG TSGELVATGH
RRLRRALVSV YDKTGLEELA AAFVEAGVEV VSTGSTADVL ARFGVAVTPV STVTGFPEVL
GGRVKTLHPH VHAGLLADLR NAEHAAVLAE LEIEPFDLLV VNLYPFRETV ASGATEDEAI
EQIDIGGPAM LRAAAKNHAS VAVVVSPDDY GDLAAAVRGT GYDLAARRRL AARAFAHTAS
YDAAVASWFA SALAPDEVAR ESGWPDVLAA QWRRTSVLRY GENPHQRAAL YVGEDGSPGL
ASARQLHGKP MSYNNYTDTD AAWRAVFDFA EPAVAVIKHA NPCGIAVAAS VAEAHRKAHA
CDPVSAFGGV IAVNRPVSVE LAEQIAEIFT EVVVAPDYEP GAVEILSRKP SIRLLLCAPP
AHPRGVEMRQ VSGGMLLQSR DALDVAGDVP AGWTLEAGAP VDDATLADLG FAWRAVRSVK
SNAILLAAGT ATVGVGMGQV NRVDAARLAV SRAGDRAKGS VAASDAFFPF PDGFQVLAEA
GVRAVVEPGG SVRDELVIEA AREAGVSLYF TGVRHFAH
//
