(data stored in ACNUC7421 zone)

HOGENOM: DESAS_1_PE10

ID   DESAS_1_PE10                         STANDARD;      PRT;   427 AA.
AC   DESAS_1_PE10; C8VVA6;
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=Adenylosuccinate synthetase; Short=AMPSase; Short=AdSS;
DE   EC=6.3.4 4;AltName: Full=IMP--aspartate ligase; (DESAS_1.PE10).
GN   Name=purA; OrderedLocusNames=Dtox_0010;
OS   DESULFOTOMACULUM ACETOXIDANS DSM 771.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=485916;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS DESAS_1.PE10.
CC       Desulfotomaculum acetoxidans DSM 771, complete genome.
CC       / IFO 0083) chromosome G, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C8VVA6_DESAS
CC   -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC       nucleotide biosynthesis (By similarity).
CC   -!- FUNCTION: Plays an important role in the de novo pathway of purine
CC       nucleotide biosynthesis. Catalyzes the first commited step in the
CC       biosynthesis of AMP from IMP (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate +
CC       N(6)-(1,2-dicarboxyethyl)-AMP.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family.
CC   -!- GENE_FAMILY: HOG000260959 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C8VVA6; -.
DR   EMBL; CP001720; ACV60975.1; -; Genomic_DNA.
DR   RefSeq; YP_003189598.1; NC_013216.1.
DR   STRING; C8VVA6; -.
DR   GeneID; 8426929; -.
DR   GenomeReviews; CP001720_GR; Dtox_0010.
DR   KEGG; dae:Dtox_0010; -.
DR   OMA; DYVVRYQ; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004019; F:adenylosuccinate synthase activity; IEA:HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00011; Adenylosucc_synth; 1; -.
DR   InterPro; IPR018220; Adenylosuccinate_synthase_AS.
DR   InterPro; IPR001114; Adenylosuccinate_synthetase.
DR   PANTHER; PTHR11846; Asucc_synthtase; 1.
DR   Pfam; PF00709; Adenylsucc_synt; 1.
DR   SMART; SM00788; Adenylsucc_synt; 1.
DR   TIGRFAMs; TIGR00184; PurA; 1.
DR   PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1.
DR   PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1.
DR   HOGENOMDNA; DESAS_1.PE10; -.
KW   Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Purine biosynthesis.
SQ   SEQUENCE   427 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSTVVLIGAQ WGDEGKGKVT DYLSERADMV VRYQGGNNAG HTVVVGDDEF KLHLIPSGIL
     YKDKLCLIGN GVVIDPSVLM EEIKGLQERG INTDNLRIST RAHVILPYHR ELDKAEEDSK
     GKNKIGTTCR GIGPTYMDKS ARVGVRIIDL MEEDRLAEIL EMNIKTKNKI LTKVYDHESF
     NFNEVFKIAK QYADNLRKYV TDTSLLINDV IDEGKNVLFE GAQGTLLDLD HGTYPYVTSS
     NPVAAGACLG AGVGPTKINK ILGVVKAYTT RVGEGPFLTE LMDNLGEMIR QNGREFGTTT
     GRPRRCGWYD AVITRYAVRI NGLTFLAVTK LDVLTGLEKL KICTGYKFED KILKDFPCSL
     KTLTKCEPVY EEMPGWQEDI SQIKNFADLP VNAQRYLNRI AELAGVPVAV IGVGMKRDQT
     IIVHELF
//

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