ID A0A1C1D0X1_9EURO Unreviewed; 546 AA.
AC A0A1C1D0X1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Bifunctional purine biosynthesis protein ADE17 {ECO:0000313|EMBL:OCT54407.1};
GN Name=ADE17 {ECO:0000313|EMBL:OCT54407.1};
GN ORFNames=CLCR_00821 {ECO:0000313|EMBL:OCT54407.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT54407.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the PurH family.
CC {ECO:0000256|ARBA:ARBA00007667}.
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:OCT54407.1}.
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DR EMBL; LGRB01000004; OCT54407.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1D0X1; -.
DR STRING; 86049.A0A1C1D0X1; -.
DR VEuPathDB; FungiDB:CLCR_00821; -.
DR VEuPathDB; FungiDB:G647_01673; -.
DR eggNOG; KOG2555; Eukaryota.
DR UniPathway; UPA00074; UER00133.
DR Proteomes; UP000094526; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01421; IMPCH; 1.
DR Gene3D; 1.10.287.440; -; 1.
DR Gene3D; 3.40.140.20; -; 2.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
DR InterPro; IPR024050; AICAR_Tfase_insert_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 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..71
FT /note="MGS-like"
FT /evidence="ECO:0000259|SMART:SM00851"
SQ SEQUENCE 546 AA; 59634 MW; B59364514804FAAE CRC64;
MLSGRVKTLH PAVHAGILAR DLASDEKDLA DQNINKVDYV VCNLYPFKDT VAKINVTIPE
AVEEIDIGGV TLIRAAAKNH SRVTILSDPA DYHHFLEELE RGEIPGESRQ RYALKAFEHT
ADYDAAISDF FRKQYAGNGV QQLSLRYGAN PHQKPASAFV RQGTLPFTVL GGSPGYINLL
DCLNAWPLVK ELKQALGLPA AASFKHVSPA GAAIAVPLSE RERQVYMVDD IEGIESSGLA
QAYARARGAD RMSSFGDMIA LSDKVDVLTA KIISREVSDG VIAPGYEPEA LALLKKKKGG
KYLVLQIDES YEPPAQETRT VYGVNLTQGR NDVKISPAET FNSIIRPKDA AASPSSSPLS
DSALRDLTVA TIAVKYTQSN SVCYALNGQV VGLGAGQQSR IHCTRLAGDK ADNWWMRFHE
RTLGIQWAKG VKRAEKSNAI DMLCSGQIDA DLSDFEKADY ERNFAEGQVP TPFTHAERRE
WLAKLSEVAV SSDAFFPFVD NVYRAARSGV KYIAAPTGSQ NDGAVFDTAE NLGITFIEQS
TRLFHH
//
