ID H6D9M6_PENBR Unreviewed; 262 AA.
AC H6D9M6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=IMP dehydrogenase type B {ECO:0000313|EMBL:AEP22338.1};
DE Flags: Fragment;
GN Name=imdB {ECO:0000313|EMBL:AEP22338.1};
OS Penicillium brevicompactum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5074 {ECO:0000313|EMBL:AEP22338.1};
RN [1] {ECO:0000313|EMBL:AEP22338.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21916847; DOI=10.1042/BJ20111278;
RA Hansen B.G., Sun X.E., Genee H.J., Kaas C.S., Nielsen J.B., Mortensen U.H.,
RA Frisvad J.C., Hedstrom L.;
RT "Adaptive evolution of drug targets in producer and non-producer
RT organisms.";
RL Biochem. J. 441:219-226(2012).
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 -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC {ECO:0000256|ARBA:ARBA00005502}.
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DR EMBL; JN112068; AEP22338.1; -; Genomic_DNA.
DR AlphaFoldDB; H6D9M6; -.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd04601; CBS_pair_IMPDH; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 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 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}; GMP biosynthesis {ECO:0000256|ARBA:ARBA00022749};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 42..101
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 105..161
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEP22338.1"
FT NON_TER 262
FT /evidence="ECO:0000313|EMBL:AEP22338.1"
SQ SEQUENCE 262 AA; 28037 MW; 5149F6F632084019 CRC64;
VTEHNMAIHM ALLGGLGVIH NNCPPDDQAE MVRKVKRYEN GFILDPVVLS PSTTVAEAKE
LKTKWNFGGF PVTEKGTLHS KLLGIVTSRD IQFHKTPEDP VTAVMSTDLV TAPAGTTLAE
ANEVLRSSKK GKLPIVDKDG LLVSLLSRSD LMKNIHYPLA SKLPSKQLLC AAAISTHDAD
KVRLQKLVDA GLDIVVVDSS QGNSMYQIAM IKWIKSTFPD IDIIAGNIVT REQAAALIAA
GADGLRIGMG SGSACITQEV MA
//