GenomeNet

Database: UniProt
Entry: A0A0P6WMM8_9CHLR
LinkDB: A0A0P6WMM8_9CHLR
Original site: A0A0P6WMM8_9CHLR 
ID   A0A0P6WMM8_9CHLR        Unreviewed;       499 AA.
AC   A0A0P6WMM8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=ADM99_12935 {ECO:0000313|EMBL:KPL71158.1};
OS   Leptolinea tardivitalis.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Leptolinea.
OX   NCBI_TaxID=229920 {ECO:0000313|EMBL:KPL71158.1, ECO:0000313|Proteomes:UP000050430};
RN   [1] {ECO:0000313|EMBL:KPL71158.1, ECO:0000313|Proteomes:UP000050430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YMTK-2 {ECO:0000313|EMBL:KPL71158.1,
RC   ECO:0000313|Proteomes:UP000050430};
RA   Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT   "Genome sequence of Leptolinea tardivitalis DSM 16556.";
RL   Submitted (JUL-2015) 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}.
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:KPL71158.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LGCK01000012; KPL71158.1; -; Genomic_DNA.
DR   RefSeq; WP_062422911.1; NZ_LGCK01000012.1.
DR   AlphaFoldDB; A0A0P6WMM8; -.
DR   STRING; 229920.ADM99_12935; -.
DR   PATRIC; fig|229920.5.peg.2912; -.
DR   OrthoDB; 9802065at2; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000050430; 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:UP000050430};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00139}.
FT   DOMAIN          1..143
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   499 AA;  54195 MW;  897C50988A63F22D CRC64;
     MPKALLSVYD KTGLVDFARG LINLGWDLLA SGGTAKLLMQ NNLKVTEVAD YTGSPEILGG
     RVKTLHPAIH GGLLARNTED DLNQLHSLGW DYIDLVAVNL YPFEATVAKP DVTLAEAIEQ
     IDIGGVALIR AAAKNHDRVT LVCDPSDYNM VLDRLTRKNL DEATRRSLAL KGFRLTSHYD
     QAISRYLDGG QGETLELYPV QSLRYGENPH QSAVLLGYHP GDTPLGGKVL QGKELSYNNL
     LDLDAAWRTV VSYKKTSIVI VKHLTPCGVA SNDDQAEAYK AAYECDTVSA YGGIIAANRP
     ITAATAEAIK DLFVECIIAP GYEPAALELF AKKKNARLIE MPDLEIEPKV EYRSVMRGVL
     RQQVDLGDPD QSGWKVVTDK QPTAEEMAAM KFAWVACQYV KSNSIVFAKG ETTVGIGGGQ
     PNRVDCVRIA ARHAGDKAKG AVMASDAFFP YPDSVEEAAK AGITAIVHPG GSIRDQISID
     LCNKLGLSMV VTGFRHFRH
//
DBGET integrated database retrieval system