(data stored in ACNUC7421 zone)

SWISSPROT: A4AVH0_MARSH

ID   A4AVH0_MARSH            Unreviewed;       490 AA.
AC   A4AVH0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 82.
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   OrderedLocusNames=FB2170_00960 {ECO:0000313|EMBL:EAR00192.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00192.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00192.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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:
CC       Reaction=H2O + IMP + NAD(+) = H(+) + NADH + XMP;
CC         Xref=Rhea:RHEA:11708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57464, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58053; EC=1.1.1.205; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01964, 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}.
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DR   EMBL; CP002157; EAR00192.1; -; Genomic_DNA.
DR   RefSeq; WP_013304887.1; NC_014472.1.
DR   STRING; 313603.FB2170_00960; -.
DR   EnsemblBacteria; EAR00192; EAR00192; FB2170_00960.
DR   KEGG; fbc:FB2170_00960; -.
DR   eggNOG; ENOG4105CP4; Bacteria.
DR   eggNOG; COG0516; LUCA.
DR   eggNOG; COG0517; LUCA.
DR   HOGENOM; HOG000165755; -.
DR   KO; K00088; -.
DR   OMA; SSMGYCG; -.
DR   OrthoDB; 532857at2; -.
DR   BioCyc; MSP313603:G1GNS-458-MONOMER; -.
DR   UniPathway; UPA00601; UER00295.
DR   Proteomes; UP000001602; 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; 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;
DR   PRODOM; A4AVH0.
DR   SWISS-2DPAGE; A4AVH0.
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
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:UP000001602}.
FT   DOMAIN       97    153       CBS. {ECO:0000259|PROSITE:PS51371}.
FT   DOMAIN      157    214       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       473    473       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       474    474       Potassium; via carbonyl oxygen; shared
FT                                with tetrameric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_01964}.
FT   METAL       475    475       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     419    419       IMP. {ECO:0000256|HAMAP-Rule:MF_01964,
FT                                ECO:0000256|PIRSR:PIRSR000130-2}.
SQ   SEQUENCE   490 AA;  52269 MW;  A8108C03794547B6 CRC64;
     MEAHQNKILG EGLTYDDVLL VPAFSEVLPR EVSIKTKFTR NISINVPIVS AAMDTVTESR
     MAIAIAQEGG IGVLHKNMTI EQQAMKVRKV KRAESGMIID PVTLPSTALV KDAKANMKEF
     SIGGIPIVDK MGKLIGIVTN RDLRFEKNNE RPLSEVMTSE NLVTVGEGTS LAEAEDILQE
     NKIEKLPVVD ANNKLVGLIT FRDITKLTQK PSANKDHFGR LRVAAAIGVT GDAVERAAAL
     VNAGVDAVVI DTAHGHTKGV VNVLKEVKNK FHKLEVIVGN IATGAAAKYL VEAGADAVKV
     GIGPGSICTT RVVAGVGFPQ FSAVLEVASA IKGSGVPVIA DGGIRYTGDI PKAIAAGADT
     VMLGSLLAGT KESPGETIIY EGRKFKSYRG MGSVEAMKHG SKDRYFQDVE DDIKKLVPEG
     IVGRVPYKGE LYESIHQFVG GLRAGMGYCG AKDIETLKES GRFVKITASG INESHPHDVT
     ITKESPNYSR
//

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