ID A0A098LKS5_9BACT Unreviewed; 508 AA.
AC A0A098LKS5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=MYP_4800 {ECO:0000313|EMBL:GAL87570.1};
OS Sporocytophaga myxococcoides.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Sporocytophaga.
OX NCBI_TaxID=153721 {ECO:0000313|EMBL:GAL87570.1, ECO:0000313|Proteomes:UP000030185};
RN [1] {ECO:0000313|EMBL:GAL87570.1, ECO:0000313|Proteomes:UP000030185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-01 {ECO:0000313|EMBL:GAL87570.1,
RC ECO:0000313|Proteomes:UP000030185};
RA Liu L., Gao P.J., Chen G.J., Wang L.S.;
RT "Sporocytophaga myxococcoides PG-01 genome sequencing.";
RL Submitted (SEP-2014) 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:GAL87570.1}.
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DR EMBL; BBLT01000014; GAL87570.1; -; Genomic_DNA.
DR RefSeq; WP_045469276.1; NZ_BBLT01000014.1.
DR AlphaFoldDB; A0A098LKS5; -.
DR STRING; 153721.MYP_4800; -.
DR eggNOG; COG0138; Bacteria.
DR OrthoDB; 9802065at2; -.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000030185; 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 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:UP000030185};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00139}.
FT DOMAIN 1..148
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 508 AA; 56516 MW; DF859DD9C45AE7B4 CRC64;
MNPRKIKSAL ISVYYKDGLD RIVKLLDKQG VKIYSTGGTQ KFIEDLGIKV TPVEELTTYP
SILGGRVKTL HPKIFGGILF RRDFEQDQKE VAQYDIPSLD LVIVDLYPFE ETVASGASDE
DIIEKIDIGG ISLIRGAAKN FKDVVIVASK DQYPMLENIL IERKGETDLN ERRLFAGRAF
DISSHYDTAI FNYFFSGEEI KHFKQSVRDF QVLRYGENPH QAGVFYGKLD DMFEKLNGKE
LSYNNLLDVD AAVGLIDEFE GTTTFAILKH NNACGIATAS SPKEAYLKAL AADPVSAFGG
VIITGSKIDI ATAEELNKLF FEVLIAPDFE KDALELLTSK KNRILLRRKS VTLPSRQFKT
LLNGVIEQEK DLKKETEEEL KPVTNRFPSD KEKRALLFAN KICKHTKSNA IVLAVDGQMI
SSGVGQTSRV DALRQAIEKA KSFGFSLEGA VMASDAFFPF PDCVEIADKA GIKAVIQPGG
SIKDQESIDY CNAHEIAMVL TGFRHFKH
//
