GenomeNet

Database: UniProt
Entry: K6VKI1_9MICO
LinkDB: K6VKI1_9MICO
Original site: K6VKI1_9MICO 
ID   K6VKI1_9MICO            Unreviewed;       615 AA.
AC   K6VKI1;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 52.
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:GAB96728.1};
GN   ORFNames=KILIM_046_00120 {ECO:0000313|EMBL:GAB96728.1};
OS   Kineosphaera limosa NBRC 100340.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC   Kineosphaera.
OX   NCBI_TaxID=1184609 {ECO:0000313|EMBL:GAB96728.1, ECO:0000313|Proteomes:UP000008366};
RN   [1] {ECO:0000313|EMBL:GAB96728.1, ECO:0000313|Proteomes:UP000008366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100340 {ECO:0000313|EMBL:GAB96728.1,
RC   ECO:0000313|Proteomes:UP000008366};
RA   Yoshida I., Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y.,
RA   Ohji S., Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Kineosphaera limosa NBRC 100340.";
RL   Submitted (AUG-2012) 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:GAB96728.1}.
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; BAHD01000046; GAB96728.1; -; Genomic_DNA.
DR   AlphaFoldDB; K6VKI1; -.
DR   STRING; 1184609.KILIM_046_00120; -.
DR   eggNOG; COG0138; Bacteria.
DR   UniPathway; UPA00074; UER00133.
DR   Proteomes; UP000008366; 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:UP000008366};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00139}.
FT   DOMAIN          78..230
FT                   /note="MGS-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51855"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          58..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  64119 MW;  85F6B830B2932F7E CRC64;
     MQQQPWAVSA TVGIRTSSGQ RSAQLVDLGA EGARPGGCNR LGGPAWVPAH ADHRSPLVTT
     EPSVSASDEG HRPDAQGGRA ADEGRRPVRR ALVSVFDKSG LAELVTGLHE AGVELVSTGG
     SAKAIADLGL PVTRVEDLTG FPECLEGRVK TLHPRVHAGL LADTRKPEHL SQLDELGVEA
     FELVAVNLYP FTQTVASGAG PDECVEQIDI GGPSMVRAAA KNHPSVAVLT SPDQYGQALE
     AVASGGFTLA QRQALAAAAF VHTATYDVAV ASWMGNVLTD TSGGSGFPQW MGATYNRLAG
     LRYGENPHQR AALYSAANGA PGLGRAEQLH GKEMSYNNYV DADAAYRAAY DHGDQPTVAI
     IKHANPCGIA VGTDVADAHA KAHACDPLSA FGGVIATNRP VTAAMAETVK DIFTEVIVAP
     GFDDDALRVL TAKKNLRLLV VQPPRPGGFE TRSIAGGLLV QERDRIDAVI EPGDDDKPTA
     GYGDRPLHWT LVAGPSVDDQ TLVDLDFAWK AVRATKSNAI LLAKGAASVG IGMGQVNRVD
     SCKLAVARAG EERAQGSVAA SDAFFPFADG PGILIDAGVK AIVAPGGSMR DDETIRACEA
     AGVSLYFTGI RHFAH
//
DBGET integrated database retrieval system