(data stored in SCRATCH zone)

SWISSPROT: C7QJ94_CATAD

ID   C7QJ94_CATAD            Unreviewed;       436 AA.
AC   C7QJ94;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 50.
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   OrderedLocusNames=Caci_0283 {ECO:0000313|EMBL:ACU69236.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69236.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69236.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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; CP001700; ACU69236.1; -; Genomic_DNA.
DR   RefSeq; WP_012784531.1; NC_013131.1.
DR   ProteinModelPortal; C7QJ94; -.
DR   STRING; 479433.Caci_0283; -.
DR   EnsemblBacteria; ACU69236; ACU69236; Caci_0283.
DR   KEGG; cai:Caci_0283; -.
DR   eggNOG; ENOG4107SGK; Bacteria.
DR   eggNOG; COG0015; LUCA.
DR   HOGENOM; HOG000033912; -.
DR   KO; K01756; -.
DR   OMA; ALIHESM; -.
DR   OrthoDB; POG091H0168; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000000851; 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   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;
DR   PRODOM; C7QJ94.
DR   SWISS-2DPAGE; C7QJ94.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:ACU69236.1};
KW   Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851}.
FT   DOMAIN      351    433       ADSL_C. {ECO:0000259|SMART:SM00998}.
SQ   SEQUENCE   436 AA;  47934 MW;  607D8CFF839D9F0B CRC64;
     MIERYTLPEM GRVWSEAHKY ELWARVETLV VEAHAAAGTI PESAVEPVRK AAPPTPEAVA
     AIEAVTQHDV IAFLSAWADN TEPREAATYV HFGMTSSDLL DTALALQLTE ATDLLLEKAD
     KLVGVLRDHA LAHRATLRVG RTHGIHGEPD VWGHRVADFA FGVARSRDRL RRAREAVGVV
     AISGAVGTYS NIDPAIETFV AAKLGMTAAD VSTQVILRDG VSEWVSALAI MATVLEAIAL
     EVRHGQRTEV RELWEPFGKG QKGSSAMPHK KNPIISERLA GLARIVRAQV VPVMEGIPLW
     HERDISHSST ERIALPDASI AVDYMLNLTI RLMSGLVVDP DRMRHNLDST GGLVYSSTVL
     LELVEMGLER DTQAYPLTQR ASMKTWETGR PFRETLREEA ATAGLAIDEA RLDEATRPER
     FVQRLDGMFE KLAKLS
//

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