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Database: UniProt/TrEMBL
Entry: Q8XJT5_CLOPE
LinkDB: Q8XJT5_CLOPE
Original site: Q8XJT5_CLOPE 
ID   Q8XJT5_CLOPE            Unreviewed;       476 AA.
AC   Q8XJT5;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   07-JAN-2015, entry version 82.
DE   RecName: Full=Adenylosuccinate lyase {ECO:0000256|RuleBase:RU361172};
DE            Short=ASL {ECO:0000256|RuleBase:RU361172};
DE            EC=4.3.2.2 {ECO:0000256|RuleBase:RU361172};
DE   AltName: Full=Adenylosuccinase {ECO:0000256|RuleBase:RU361172};
GN   Name=purB {ECO:0000313|EMBL:BAB81374.1};
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102 {ECO:0000313|EMBL:BAB81374.1, ECO:0000313|Proteomes:UP000000818};
RN   [1] {ECO:0000313|EMBL:BAB81374.1, ECO:0000313|Proteomes:UP000000818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A {ECO:0000313|Proteomes:UP000000818};
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A.,
RA   Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic
RT   flesh-eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-
CC       (5-phospho-D-ribosyl)imidazole-4-carboxamide.
CC       {ECO:0000256|RuleBase:RU361172}.
CC   -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
CC       {ECO:0000256|RuleBase:RU361172}.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 2/2. {ECO:0000256|RuleBase:RU361172}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
CC       {ECO:0000256|RuleBase:RU361172}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000256|RuleBase:RU361172}.
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DR   EMBL; BA000016; BAB81374.1; -; Genomic_DNA.
DR   RefSeq; NP_562584.1; NC_003366.1.
DR   ProteinModelPortal; Q8XJT5; -.
DR   SMR; Q8XJT5; 4-465.
DR   STRING; 195102.CPE1668; -.
DR   EnsemblBacteria; BAB81374; BAB81374; BAB81374.
DR   GeneID; 989978; -.
DR   KEGG; cpe:CPE1668; -.
DR   PATRIC; 19497287; VBICloPer59675_1739.
DR   HOGENOM; HOG000033915; -.
DR   KO; K01756; -.
DR   OMA; IHSQLDH; -.
DR   OrthoDB; EOG686NDB; -.
DR   BioCyc; CPER195102:GJFM-1715-MONOMER; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.275.10; -; 1.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR004769; Pur_lyase.
DR   PANTHER; PTHR11444; PTHR11444; 1.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00928; purB; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000818};
KW   Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:BAB81374.1};
KW   Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000818}.
SQ   SEQUENCE   476 AA;  53830 MW;  EDB5D4019C833B44 CRC64;
     MKNLYSTPLN SRYASKEMSY IFSDDMKFST WRKLWVALAE GEKELGLNIT DEQIEELKSH
     ISDINYEEAI KKEKEVRHDV MSHVYAYGLQ CPSAKGIIHL GATSCYVGDN TDVIIMRDAL
     LLIKKKIVAV LNNLKRFALE YKDMPTLGFT HFQPAQLTTV GKRATLWMQD LVMDMENIDF
     LLSTLKLRGV KGTTGTQASF MNLFEGDEEK VKALDKIVAE KMGFKKSFGV TGQTYPRKLD
     SIILNTLSEI AQSAYKFSND LRLLQSMKEI EEPFEKNQIG SSAMAYKRNP MRSERMGALA
     RYVIVDALNP AITASTQWFE RTLDDSANKR IAVAEAFLAL DGVLYLYINI AENMVVYDKV
     IEAHVNQELP FMATENIMME SVKKGGDRQE LHERIRVHSM DAAQRVKGEG LNNDLIERII
     NDPSFNLSKE EIIAIIDPVK FVGRAPSQVV EFIDEYVNPI IEANKDAASL SSDITV
//
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