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Database: UniProt
Entry: H6D9M6_PENBR
LinkDB: H6D9M6_PENBR
Original site: H6D9M6_PENBR 
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
//
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