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Database: UniProt
Entry: A0A0G3XCP1_9SPHN
LinkDB: A0A0G3XCP1_9SPHN
Original site: A0A0G3XCP1_9SPHN 
ID   A0A0G3XCP1_9SPHN        Unreviewed;       530 AA.
AC   A0A0G3XCP1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ECO:0000313|EMBL:AKM08957.1};
GN   ORFNames=AB433_01555 {ECO:0000313|EMBL:AKM08957.1}, GGR19_000653
GN   {ECO:0000313|EMBL:MBB3989252.1};
OS   Croceicoccus naphthovorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceicoccus.
OX   NCBI_TaxID=1348774 {ECO:0000313|EMBL:AKM08957.1, ECO:0000313|Proteomes:UP000035287};
RN   [1] {ECO:0000313|EMBL:AKM08957.1, ECO:0000313|Proteomes:UP000035287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PQ-2 {ECO:0000313|EMBL:AKM08957.1,
RC   ECO:0000313|Proteomes:UP000035287};
RA   Zeng Y., Huang Y.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB3989252.1, ECO:0000313|Proteomes:UP000536420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 102796 {ECO:0000313|EMBL:MBB3989252.1,
RC   ECO:0000313|Proteomes:UP000536420};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2020) 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; CP011770; AKM08957.1; -; Genomic_DNA.
DR   EMBL; JACIEL010000003; MBB3989252.1; -; Genomic_DNA.
DR   RefSeq; WP_047819653.1; NZ_JACIEL010000003.1.
DR   AlphaFoldDB; A0A0G3XCP1; -.
DR   STRING; 1348774.AB433_01555; -.
DR   KEGG; cna:AB433_01555; -.
DR   PATRIC; fig|1348774.3.peg.328; -.
DR   OrthoDB; 9802065at2; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000035287; Chromosome.
DR   Proteomes; UP000536420; 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:UP000035287};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00139}.
FT   DOMAIN          1..149
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   530 AA;  56110 MW;  F7C0B9985F414A4A CRC64;
     MQDPVTIRRA LLSVSDKTGL VELGQALAAR KVELVSTGGT AKALREAGLT VKDISDLTGF
     PEMMDGRVKT LHPMVHGGLL AVRDNPEHAK AMQDHAIGAI DLVVVNLYPF VQTVASGADR
     DTIIENIDIG GPSMVRSAAK NHAYVTLLTD PDDYAALITE MDAGVGATSF DFRKMLAAKA
     FAATAAYDAA IASWFAHADQ GQKFPPRRSV AAKLVSTLRY GENPHQDAAL YVPEGPHVMG
     LPQAEQVQGK ELSYNNYNDA NAALELVAEF RDGPPTVVIV KHANPCGVAT GETLVEAWDK
     ALACDSVSAF GGIVAVNRPL DVATAEAISK IFTEVVVAPG ASDEAKAVFA KKKNLRLLIT
     QGLPDPRRVG QNITIIAGGM LQQDRDNGAV DPAALKVVTK REPTEQELKD CLFAWTVARH
     VKSNAIVYAK DGQTAGIGAG QMNRRDSARI AAAKAMEAAE TMGWDMPLTH GSAVASDAFF
     PFADGLLSAA EAGATAVIQP GGSIRDEEVI AAADEKGIAM VFTGMRHFRH
//
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