ID   A0A1B9AXB3_9BACI        Unreviewed;       488 AA.
AC   A0A1B9AXB3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   12-SEP-2018, entry version 10.
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   ORFNames=A8L44_18290 {ECO:0000313|EMBL:OCA88383.1};
OS   Bacillus sp. FJAT-27986.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA88383.1, ECO:0000313|Proteomes:UP000092673};
RN   [1] {ECO:0000313|EMBL:OCA88383.1, ECO:0000313|Proteomes:UP000092673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA88383.1,
RC   ECO:0000313|Proteomes:UP000092673};
RA   Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y.,
RA   Wang J., Liu B., Liu G.;
RT   "Bacillus sp. FJAT-27986.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP)
CC       to xanthosine 5'-phosphate (XMP), the first committed and rate-
CC       limiting step in the de novo synthesis of guanine nucleotides, and
CC       therefore plays an important role in the regulation of cell
CC       growth. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC   -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
CC       xanthosine 5'-phosphate + NADH. {ECO:0000256|HAMAP-Rule:MF_01964,
CC       ECO:0000256|RuleBase:RU003928}.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01964};
CC   -!- ACTIVITY REGULATION: Mycophenolic acid (MPA) is a non-competitive
CC       inhibitor that prevents formation of the closed enzyme
CC       conformation by binding to the same site as the amobile flap. In
CC       contrast, mizoribine monophosphate (MZP) is a competitive
CC       inhibitor that induces the closed conformation. MPA is a potent
CC       inhibitor of mammalian IMPDHs but a poor inhibitor of the
CC       bacterial enzymes. MZP is a more potent inhibitor of bacterial
CC       IMPDH. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
CC       XMP 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. {ECO:0000256|HAMAP-
CC       Rule:MF_01964, ECO:0000256|RuleBase:RU003927}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01964}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OCA88383.1}.
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DR   EMBL; MAYV01000007; OCA88383.1; -; Genomic_DNA.
DR   RefSeq; WP_066103306.1; NZ_MAYV01000007.1.
DR   EnsemblBacteria; OCA88383; OCA88383; A8L44_18290.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000092673; Unassembled WGS sequence.
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; cd00381; IMPDH; 1.
DR   Gene3D; 3.20.20.70; -; 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   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000130; IMPDH; 1.
DR   SMART; SM00116; CBS; 2.
DR   TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000092673};
KW   GMP biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003928};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003928};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01964, ECO:0000256|PIRSR:PIRSR000130-3,
KW   ECO:0000256|RuleBase:RU003928};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003927};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|PIRSR:PIRSR000130-4, ECO:0000256|RuleBase:RU003928};
KW   Purine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01964,
KW   ECO:0000256|RuleBase:RU003928};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092673}.
FT   DOMAIN       95    156       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   DOMAIN      157    215       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   NP_BIND     251    253       NAD. {ECO:0000256|PIRSR:PIRSR000130-3}.
FT   NP_BIND     301    303       NAD. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-3}.
FT   REGION      341    343       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                2}.
FT   REGION      364    365       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                2}.
FT   REGION      388    392       IMP binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                2}.
FT   ACT_SITE    308    308       Thioimidate intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-1}.
FT   ACT_SITE    404    404       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01964, ECO:0000256|PIRSR:PIRSR000130-
FT                                1}.
FT   METAL       303    303       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       305    305       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       308    308       Potassium; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-4}.
FT   METAL       470    470       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       471    471       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       472    472       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   BINDING     251    251       NAD. {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   BINDING     306    306       IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-2}.
FT   BINDING     416    416       IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-2}.
SQ   SEQUENCE   488 AA;  53087 MW;  5086ED0AF5ED632C CRC64;
     MWKDKFSKEG LTFDDVLLIP GKSEVLPKDV SLKVSLADNL ALNIPIISAG MDTVTESEMA
     IAMARQGGLG VIHKNMSIEQ QAEQVDKVKR SENGVITKPF FLTPENQVYD AEHLMGKYRI
     SGVPIVNNKE EKKLVGIITN RDMRFIRDYS MRIDDVMTKE NLVTAPVGTN LEEAQKILQQ
     YKIEKLPLVD EEGTLQGLIT IKDIEKIIEF PRSAKDKYGR LLVAAAVGVT SDTMKRVEML
     VSADVDAIVL DTAHGHSKGV LDKVREIRET FPELTIIAGN VATAEGTRAL IEAGADIVKV
     GIGPGSICTT RVVAGVGVPQ ITAIYDCATE ARKHGKSIIA DGGIKYSGDV AKALAAGGHA
     VMLGSLLAGV TESPGDTEIF QGRRFKVYRG MGSVAAMEKG SKDRYFQEDA KKFVPEGIEG
     RIPYKGPLAD TIYQLIGGLR AGMGYCGTKD LEELRENSQF VRMTGAGLKE SHPHDVQITK
     EAPNYSYN
//