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Database: UniProt
Entry: A0A1W2AR55_9FLAO
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ID   A0A1W2AR55_9FLAO        Unreviewed;       505 AA.
AC   A0A1W2AR55;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=SAMN02787074_2158 {ECO:0000313|EMBL:SMC63010.1};
OS   Chryseobacterium sp. YR221.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1500293 {ECO:0000313|EMBL:SMC63010.1, ECO:0000313|Proteomes:UP000192341};
RN   [1] {ECO:0000313|EMBL:SMC63010.1, ECO:0000313|Proteomes:UP000192341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR221 {ECO:0000313|EMBL:SMC63010.1,
RC   ECO:0000313|Proteomes:UP000192341};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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; FWXM01000003; SMC63010.1; -; Genomic_DNA.
DR   RefSeq; WP_047485328.1; NZ_FWXM01000003.1.
DR   AlphaFoldDB; A0A1W2AR55; -.
DR   STRING; 1500293.SAMN02787074_2158; -.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000192341; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00139}.
FT   DOMAIN          1..145
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
SQ   SEQUENCE   505 AA;  56377 MW;  436419A7C8F4ED03 CRC64;
     MSKKRVLISV SDKSGLIEFA QFLEAQNYEL ISTGGTFKHL KDAGLNPIQI DEVTNFPEML
     DGRVKTLHPK VHGGLLAVRT NEEHMKTVQE HGIGLIDMVI VNLYPFFENV NKDISLHEKV
     EFIDIGGPSM LRSAAKNFDS VTVITDVEDY TAVKLEMEQN GDTYIETRKK LAGKVFNLTS
     AYDAAISRML LDEEYPTYLN ASYKKVSDLR YGENPHQTAA YYVSTFENGA MKDFEQLGGK
     ELSFNNLRDM DLCWKVVTEF KEEMACCAVK HSTPCGVAIG TSALETYQKT FECDPVSIFG
     GIVAMNYTIN AATAEELNKT FLEIVMAPDF DEEALEVLRK KKNLRIIKIV NPVSDKQTWV
     KVDGGILVQD NDTYFSDDIK VVTEVQPTEE QKKALLFSQR VVKYVKSNAI VVSNGVQAFG
     IGGGQVNRIW ATQQAIERAK EKFSGDLVLA SDAFFPFRDV VDFCAQEGIK AIIQPGGSVK
     DQDSVEAANE HGIPMMFTGV RHFFH
//
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