(data stored in SCRATCH zone)

SWISSPROT: D6ZA92_SEGRD

ID   D6ZA92_SEGRD            Unreviewed;       476 AA.
AC   D6ZA92;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, 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=Srot_0145 {ECO:0000313|EMBL:ADG96634.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96634.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96634.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
CC         carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide + fumarate;
CC         Xref=Rhea:RHEA:23920, ChEBI:CHEBI:29806, ChEBI:CHEBI:58443,
CC         ChEBI:CHEBI:58475; EC=4.3.2.2;
CC         Evidence={ECO:0000256|RuleBase:RU361172};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate;
CC         Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567,
CC         ChEBI:CHEBI:456215; EC=4.3.2.2;
CC         Evidence={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; CP001958; ADG96634.1; -; Genomic_DNA.
DR   RefSeq; WP_013137090.1; NC_014168.1.
DR   STRING; 640132.Srot_0145; -.
DR   EnsemblBacteria; ADG96634; ADG96634; Srot_0145.
DR   KEGG; srt:Srot_0145; -.
DR   eggNOG; ENOG4107SGK; Bacteria.
DR   eggNOG; COG0015; LUCA.
DR   HOGENOM; HOG000033913; -.
DR   KO; K01756; -.
DR   OMA; ASSCEKI; -.
DR   OrthoDB; 347727at2; -.
DR   BioCyc; SROT640132:G1GLH-149-MONOMER; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   Proteomes; UP000002247; 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   InterPro; IPR019468; AdenyloSucc_lyase_C.
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; D6ZA92.
DR   SWISS-2DPAGE; D6ZA92.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:ADG96634.1};
KW   Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247}.
FT   DOMAIN      369    454       ADSL_C. {ECO:0000259|SMART:SM00998}.
SQ   SEQUENCE   476 AA;  51846 MW;  FF818477A2635243 CRC64;
     MSTPQTPDVL AARYATKELV ALWSPRARVV LERDLWIAVL KAQIELGVPG GDAASVADYE
     RVKEQVDLDS IAARERVTRH DVKARIDEFN ALAGHELVHR GMTSRDATEN VEQSVIRASL
     AHVRDHAVAA LARLAERAAQ YAPTMLVARS HNVPAQATTL GKRFATCAQE LLIAVRRVDE
     LIERYPLRGI QGPVGTAQDM LDLLGGDRDK FARLQRSVAE HVGFTQALVS VGQIYPRSLD
     HDVVSALVQL AAAPSSFAHT LRLMAGQELA TEGFQPGQVG SSAMPHKTNP RTSERINGLA
     VVLRGYASMT AELAGAQWNE GDVFCSVVRR VALPDAFYAI DGLFEGFLTV LGEFHAFEPV
     IEREVARYLP FLGTTRILMA AVRAGVGREA AHEAIKEHAV ALANDIRERG AEPDLLSRLA
     QDQRLGLTRA QLDEALADRD LFLGAADDQV RRVIDEVEAL VAKHPEAAAY RPGSIL
//

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