ID A0A0B6TDS0_9CORY Unreviewed; 506 AA.
AC A0A0B6TDS0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
DE Short=IMP dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01964};
DE Short=IMPD {ECO:0000256|HAMAP-Rule:MF_01964};
DE Short=IMPDH {ECO:0000256|HAMAP-Rule:MF_01964};
DE EC=1.1.1.205 {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
GN Name=guaB {ECO:0000256|HAMAP-Rule:MF_01964,
GN ECO:0000313|EMBL:AJK68077.1};
GN ORFNames=B840_02245 {ECO:0000313|EMBL:AJK68077.1};
OS Corynebacterium marinum DSM 44953.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224162 {ECO:0000313|EMBL:AJK68077.1, ECO:0000313|Proteomes:UP000031928};
RN [1] {ECO:0000313|EMBL:AJK68077.1, ECO:0000313|Proteomes:UP000031928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44953 {ECO:0000313|EMBL:AJK68077.1,
RC ECO:0000313|Proteomes:UP000031928};
RA Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT "Complete genome sequence of Corynebacterium marinum DSM 44953.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) to
CC xanthosine 5'-phosphate (XMP), the first committed and rate-limiting
CC step in the de novo synthesis of guanine nucleotides, and therefore
CC plays an important role in the regulation of cell growth.
CC {ECO:0000256|HAMAP-Rule:MF_01964}.
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|HAMAP-Rule:MF_01964, ECO:0000256|RuleBase:RU003928};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958,
CC ECO:0000256|HAMAP-Rule:MF_01964};
CC -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive
CC inhibitor that prevents formation of the closed enzyme conformation by
CC binding to the same site as the amobile flap. In contrast, mizoribine
CC monophosphate (MZP) is a competitive inhibitor that induces the closed
CC conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor
CC inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of
CC bacterial IMPDH. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; XMP
CC from IMP: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01964,
CC ECO:0000256|RuleBase:RU003928}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC {ECO:0000256|ARBA:ARBA00005502, ECO:0000256|HAMAP-Rule:MF_01964,
CC ECO:0000256|RuleBase:RU003927}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01964}.
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DR EMBL; CP007790; AJK68077.1; -; Genomic_DNA.
DR RefSeq; WP_042620772.1; NZ_CP007790.1.
DR AlphaFoldDB; A0A0B6TDS0; -.
DR STRING; 1224162.B840_02245; -.
DR KEGG; cmq:B840_02245; -.
DR HOGENOM; CLU_022552_1_2_11; -.
DR OrthoDB; 9805398at2; -.
DR UniPathway; UPA00601; UER00295.
DR Proteomes; UP000031928; Chromosome.
DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-UniRule.
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, ECO:0000256|HAMAP-
KW Rule:MF_01964};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01964};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01964};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964,
KW ECO:0000256|RuleBase:RU003927};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01964};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01964}; Reference proteome {ECO:0000313|Proteomes:UP000031928}.
FT DOMAIN 105..163
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 165..222
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT ACT_SITE 317
FT /note="Thioimidate intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-1"
FT ACT_SITE 422
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-1"
FT BINDING 259..261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 259
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT BINDING 310..312
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-3"
FT BINDING 312
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|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-4"
FT BINDING 314
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|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-4"
FT BINDING 315
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-2"
FT BINDING 317
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|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-4"
FT BINDING 350..352
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-2"
FT BINDING 373..374
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-2"
FT BINDING 397..401
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-2"
FT BINDING 437
FT /ligand="IMP"
FT /ligand_id="ChEBI:CHEBI:58053"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964,
FT ECO:0000256|PIRSR:PIRSR000130-2"
FT BINDING 490
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT BINDING 491
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
FT BINDING 492
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /ligand_note="ligand shared between two tetrameric
FT partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01964"
SQ SEQUENCE 506 AA; 53510 MW; 0E0C01D1A48FAF7C CRC64;
MTHQRVSTGG DDPDKVALLG LTFDDVLLLP AESNIVPSEV DTSTMFTRNL RLGVPIISAA
MDTVTEARMA VAMARQGGLG VLHRNLSAEE QAEQVEIVKR SESGMVTDPV TCTPDMTIGE
VDALCARFRI SGLPVVDENG ILVGICTNRD MRFEPNPDRR VAEVMTPMPL VVAPEGVTKE
QALELLSTKK VEKLPIVDGA GKLVGLITVK DFVKTEQHPN ASKDEQGRLL VAAGIGTGDE
SWGRAGQLVE AGVDVLVVDS AHAHNNRVLE MVSRVKKDFG DRVDVVGGNL ATRSAAQAMI
DAGADAIKVG IGPGSICTTR VVAGVGAPQI TAIMEASVPA RKAGVPIIAD GGMQFSGDVA
KALAAGASSV MLGSMLAGTT EAPGDVVVVN GKQYKRYRGM GSMGAMQGRG LSGEKRSYSK
DRYFQADVRS EDKLVPEGIE GRVPFRGSIE QITHQLVGGL RAAMGYTGST TVKDLQTKQF
VQITSAGLKE SHPHHIQQTV EAPNYH
//
