ID G5BHA1_HETGA Unreviewed; 504 AA.
AC G5BHA1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 ORFNames=GW7_16805 {ECO:0000313|EMBL:EHB08662.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB08662.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB08662.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(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|RuleBase:RU003928};
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|RuleBase:RU003927}.
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; JH170314; EHB08662.1; -; Genomic_DNA.
DR AlphaFoldDB; G5BHA1; -.
DR STRING; 10181.G5BHA1; -.
DR eggNOG; KOG2550; Eukaryota.
DR InParanoid; G5BHA1; -.
DR UniPathway; UPA00601; UER00295.
DR Proteomes; UP000006813; Unassembled WGS sequence.
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; 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:SF74; INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE 1; 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; SSF51412; Inosine monophosphate dehydrogenase (IMPDH); 2.
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|RuleBase:RU003928};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003928};
KW NAD {ECO:0000256|PIRSR:PIRSR000130-3, ECO:0000256|RuleBase:RU003928};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003927};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|PIRSR:PIRSR000130-4};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU003928};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813}.
FT DOMAIN 110..169
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 175..233
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 327
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-1"
FT BINDING 270..272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 320..322
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 322
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 324
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 327
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:EHB08662.1"
SQ SEQUENCE 504 AA; 54384 MW; 789771ADF950F1D1 CRC64;
EDGLTAQQLF AHADGLTYND FLILPGFIDF IADEVDLTSA LTRKITLKTP LISSPMDTVT
EADMAIAMAL MGGIGFIHHN CTPEFQANEV RKVKATFSFP FCPQKFEQGF ITDPVVLSPS
HTVGDVLEAK IRHGFSGIPI TETGTMGSKL VGIVTSRDID FLAEKDHTTL LTEVMTPRME
LVVAPAGVTL KEANEILQRS KKGKLPIVND RDELVAIIAR TDLKKNRDYP LASKDSHKQL
LCGAAVGTRE DDKYRLDLLT QAGADVIVLD SSQGNSVYQI AMVHYIKQKY PHLQVIGGNV
VTAAQAKNLI DAGVDGLRVG MGCGSICITQ EVMACGRPQG TAVYKVAEYA RRFGVPVIAD
GGIQTVGHVV KALALGASTV MMGSLLAATT EAPGEYFFSD GVRLKKYRGM GSLDAMEKCS
SSQKRYFSEG DKVKIAQGVS GSIQDKGSIQ KFVPYLIAGI QHGCQDIGAR SLSVLRSMMY
SGELKFEKRT MSAQIEGGVH SLHS
//
