(data stored in ACNUC30567 zone)

HOGENOM: ARATH_2_PE4129

ID   ARATH_2_PE4129                       STANDARD;      PRT;   839 AA.
AC   ARATH_2_PE4129; O80452; B9DFX9; Q56XX1; Q93ZR9;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=AMP deaminase; Short=AtAMPD; EC=3.5.4 6;AltName:
DE   Full=Protein EMBRYONIC FACTOR 1; (ARATH_2.PE4129).
GN   Name=AMPD; Synonyms=FAC1; OrderedLocusNames=At2g38280;
OS   ARABIDOPSIS THALIANA.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC   eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARATH_2.PE4129.
CC       Arabidopsis thaliana chromosome 2 TAIR10 full sequence 1..19698289
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:AMPD_ARATH
CC   -!- FUNCTION: AMP deaminase plays a critical role in energy
CC       metabolism. Essential for the transition from zygote to embryo.
CC   -!- CATALYTIC ACTIVITY: AMP + H(2)O = IMP + NH(3).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit.
CC   -!- ENZYME REGULATION: Activated by ATP. Activated by sulfate ions (in
CC       vitro). Inhibited by phosphate ions.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6.7 mM for AMP (in the absence of ATP);
CC         KM=0.26 mM for AMP (in the presence of 1 mM ATP);
CC         Vmax=17 umol/min/mg enzyme (in the absence of ATP);
CC         Vmax=375 umol/min/mg enzyme (in the presence of 1 mM ATP);
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC       IMP from AMP: step 1/1.
CC   -!- SUBUNIT: Homodimer. Interacts with AHK4.
CC   -!- INTERACTION:
CC       Q9C5U0:AHK4; NbExp=2; IntAct=EBI-1807679, EBI-1100775;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein.
CC       Microsome membrane. Note=Might be associated with the inner
CC       mitochondrial membrane (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves,
CC       flowers, pollen grains, pollen tubes and siliques, and at a lower
CC       level in stems.
CC   -!- DEVELOPMENTAL STAGE: Expressed in both male and female
CC       gametophytes, at the zygote stage, in the endosperm, and during
CC       early embryo development. Observed in cotyledonary embryos and in
CC       the basal part of the embryo, but not in the suspensor or in
CC       mature embryos. Also expressed during somatic embryogenesis.
CC   -!- SIMILARITY: Belongs to the adenosine and AMP deaminases family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD94943.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC   -!- GENE_FAMILY: HOG000092200 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT2G38280;AT2G38280.1;AT2G38280.1.
DR   EMBL; AC003028; - ;
DR   EMBL; AK221552; - ;
DR   EMBL; AK316943; - ;
DR   EMBL; AY056301; - ;
DR   EMBL; AY133852; - ;
DR   UniProtKB/Swiss-Prot; O80452; B9DFX9; Q56XX1; Q93ZR9; -.
DR   EMBL; AC003028; AAC27176.2; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09516.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09517.1; -; Genomic_DNA.
DR   EMBL; AY056301; AAL07150.1; -; mRNA.
DR   EMBL; AY133852; AAM91786.1; -; mRNA.
DR   EMBL; AK316943; BAH19646.1; -; mRNA.
DR   EMBL; AK221552; BAD94943.1; ALT_SEQ; mRNA.
DR   IPI; IPI00546126; -.
DR   PIR; T01259; T01259.
DR   RefSeq; NP_565886.1; NM_129384.2.
DR   RefSeq; NP_850294.1; NM_179963.2.
DR   UniGene; At.12466; -.
DR   PDB; 2A3L; X-ray; 3.34 A; A=140-839.
DR   PDBsum; 2A3L; -.
DR   ProteinModelPortal; O80452; -.
DR   SMR; O80452; 212-839.
DR   IntAct; O80452; 2.
DR   STRING; O80452; -.
DR   PRIDE; O80452; -.
DR   EnsemblPlants; AT2G38280.1; AT2G38280.1; AT2G38280.
DR   EnsemblPlants; AT2G38280.2; AT2G38280.2; AT2G38280.
DR   GeneID; 818408; -.
DR   GenomeReviews; CT485783_GR; AT2G38280.
DR   KEGG; ath:AT2G38280; -.
DR   NMPDR; fig|3702.1.peg.10940; -.
DR   TAIR; At2g38280; -.
DR   eggNOG; KOG1096; -.
DR   GeneTree; EPGT00070000029639; -.
DR   InParanoid; O80452; -.
DR   OMA; TIDPASH; -.
DR   PhylomeDB; O80452; -.
DR   ProtClustDB; PLN02768; -.
DR   ArrayExpress; O80452; -.
DR   Genevestigator; O80452; -.
DR   GermOnline; AT2G38280; Arabidopsis thaliana.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0003876; F:AMP deaminase activity; IGI:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0009737; P:response to abscisic acid stimulus; IDA:TAIR.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A/AMP_deaminase.
DR   InterPro; IPR006329; AMP_deaminase.
DR   Pfam; PF00962; A_deaminase; 1.
DR   TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
DR   HOGENOMDNA; ARATH_2.PE4129; -.
KW   AT2G38280pg.C_scaffold_1320000031; AT2G38280.1.C_scaffold_1320000031;
KW   AC003028; AK221552; AK316943; AY056301; AY133852;
KW   3D-structure; Allosteric enzyme; ATP-binding; Complete proteome;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Metal-binding; Microsome;
KW   Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Zinc.
SQ   SEQUENCE   839 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MEPNIYQLAL AALFGASFVA VSGFFMHFKA LNLVLERGKE RKENPDGDEP QNPTLVRRRS
     QVRRKVNDQY GRSPASLPDA TPFTDGGGGG GGDTGRSNGH VYVDEIPPGL PRLHTPSEGR
     ASVHGASSIR KTGSFVRPIS PKSPVASASA FESVEESDDD DNLTNSEGLD ASYLQANGDN
     EMPADANEEQ ISMAASSMIR SHSVSGDLHG VQPDPIAADI LRKEPEQETF VRLNVPLEVP
     TSDEVEAYKC LQECLELRKR YVFQETVAPW EKEVISDPST PKPNTEPFAH YPQGKSDHCF
     EMQDGVVHVF ANKDAKEDLF PVADATAFFT DLHHVLKVIA AGNIRTLCHR RLVLLEQKFN
     LHLMLNADKE FLAQKSAPHR DFYNVRKVDT HVHHSACMNQ KHLLRFIKSK LRKEPDEVVI
     FRDGTYLTLR EVFESLDLTG YDLNVDLLDV HADKSTFHRF DKFNLKYNPC GQSRLREIFL
     KQDNLIQGRF LGEITKQVFS DLEASKYQMA EYRISIYGRK MSEWDQLASW IVNNDLYSEN
     VVWLIQLPRL YNIYKDMGIV TSFQNILDNI FIPLFEATVD PDSHPQLHVF LKQVVGFDLV
     DDESKPERRP TKHMPTPAQW TNAFNPAFSY YVYYCYANLY VLNKLRESKG MTTITLRPHS
     GEAGDIDHLA ATFLTCHSIA HGINLRKSPV LQYLYYLAQI GLAMSPLSNN SLFLDYHRNP
     FPVFFLRGLN VSLSTDDPLQ IHLTKEPLVE EYSIAASVWK LSACDLCEIA RNSVYQSGFS
     HALKSHWIGK DYYKRGPDGN DIHKTNVPHI RVEFRDTIWK EEMQQVYLGK AVISDEVVP
//

If you have problems or comments...

PBIL Back to PBIL home page