ID G4WT14_9EURO Unreviewed; 527 AA.
AC G4WT14;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|RuleBase:RU003928};
DE EC=1.1.1.205 {ECO:0000256|RuleBase:RU003928};
DE Flags: Fragment;
GN Name=imdA {ECO:0000313|EMBL:AEP94205.1};
OS Penicillium carneum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=47248 {ECO:0000313|EMBL:AEP94205.1};
RN [1] {ECO:0000313|EMBL:AEP94205.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 3472 {ECO:0000313|EMBL:AEP94205.1};
RA Hansen B.G., Genee H.J., Kaas C.S., Nielsen J.B., Requeira T.B.,
RA Mortensen U.H., Frisvad J.C., Patil K.R.;
RT "A new class of IMP dehydrogenase with a role in self-resistance of
RT mycophen= olic acid producing fungi.";
RL Appl. Environ. Microbiol. 11:202-202(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP; Xref=Rhea:RHEA:11708,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57464,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58053;
CC EC=1.1.1.205; Evidence={ECO:0000256|ARBA:ARBA00024264,
CC ECO:0000256|RuleBase:RU003928};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC from IMP: step 1/1. {ECO:0000256|RuleBase:RU003928}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|RuleBase:RU003927}.
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DR EMBL; JF302656; AEP94205.1; -; Genomic_DNA.
DR AlphaFoldDB; G4WT14; -.
DR UniPathway; UPA00601; UER00295.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04601; CBS_pair_IMPDH; 1.
DR CDD; cd00381; IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01964; IMPDH; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005990; IMP_DH.
DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR InterPro; IPR001093; IMP_DH_GMPRt.
DR NCBIfam; TIGR01302; IMP_dehydrog; 1.
DR PANTHER; PTHR11911:SF111; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11911; INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF00478; IMPDH; 1.
DR PIRSF; PIRSF000130; IMPDH; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01240; IMPDH; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749,
KW ECO:0000256|RuleBase:RU003928};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003928};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000130-3};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003927};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000130-4};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755,
KW ECO:0000256|RuleBase:RU003928}.
FT DOMAIN 125..187
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 188..244
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 339
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT ACT_SITE 450
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT BINDING 282..284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 332..334
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 334
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT BINDING 336
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT BINDING 339
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEP94205.1"
FT NON_TER 527
FT /evidence="ECO:0000313|EMBL:AEP94205.1"
SQ SEQUENCE 527 AA; 55684 MW; 8D00C2E149530CF6 CRC64;
GAAMKAEIAD YTKAVEILDT YTTLDGLDAD TLLDSDKHGA LTYNDFLILP GYIGFPASDV
SLDTPVTKRI SLKAPLLSSP MDTVTEHNMA IHMALLGGLG VIHHNCSPED QAEMVRKVKR
YENGFILDPV VISPKATVGE VKELKAKWGF GGFPVTENGT LKSKLVGMVT SRDIQFHTGL
DEPVTAVMAT DLVTAPAGTT LAEANEVLRR SKKGKLPIID PNGNIVALLS RSDLMKNLHY
PLASKLPDSK QLIAAAAIGT REEDKKRLQL LVEAGLDIVI LDSSQGNSMY QIEMIKYIKK
TIPEVDVIGG NVVTREQAAA LIAAGVDGLR IGMGSGSACI TQEVMAVGRP QAASVRSVAT
FAARFGVPCI ADGGIQNVGH IVKGLAMGAS TIMMGGLLAG TTESPGEYFV SNEGQLVKAY
RGMGSIAAME DKKAGGDGKD SKASNAGTAR YFSEKDRVLV AQGVAGSVLD RGSVTKFIPY
LIAGVQHSLQ DIGVKSLTDM HDGVNKGTVR FEMRSASAMT EGNVHGL
//
