ID D6YTD8_WADCW Unreviewed; 468 AA.
AC D6YTD8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:ADI37399.1};
GN OrderedLocusNames=wcw_0022 {ECO:0000313|EMBL:ADI37399.1};
OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI37399.1, ECO:0000313|Proteomes:UP000001505};
RN [1] {ECO:0000313|EMBL:ADI37399.1, ECO:0000313|Proteomes:UP000001505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT "The Waddlia genome: a window into chlamydial biology.";
RL PLoS ONE 5:E10890-E10890(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; Xref=Rhea:RHEA:23920,
CC ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, 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; AMP
CC from IMP: step 2/2. {ECO:0000256|RuleBase:RU361172}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC 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; CP001928; ADI37399.1; -; Genomic_DNA.
DR AlphaFoldDB; D6YTD8; -.
DR STRING; 716544.wcw_0022; -.
DR KEGG; wch:wcw_0022; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_1_1_0; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000001505; Chromosome.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate 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 CDD; cd03302; Adenylsuccinate_lyase_2; 1.
DR Gene3D; 1.10.275.60; -; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
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 NCBIfam; TIGR00928; purB; 1.
DR PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 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; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:ADI37399.1};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW Reference proteome {ECO:0000313|Proteomes:UP000001505}.
FT DOMAIN 373..457
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 468 AA; 52901 MW; AE9EC44E347645C7 CRC64;
MQNEIADLYQ SPLTSRYASV EMSRLFSPQF KHSTWRRLWV ALAESEKELG LDISQKQIDE
MTSCIESIDF GLAHRYESQL HHDVMAHIYA YGDQCPSARS IIHLGATSCF VTDNTDTIQA
KQALSLLISR LKQVITNLAD FSLRNKETAC LGFTHFQPAQ LTTVGKRASL WTQDLFMDLE
ELSYRKSRLR FLGVKGATGT QASFLSLFNG NHDKVKQLDE RVSEKMGFDR RFPVSGQTYT
RKQDTQTLNA MADLGASCHK FATDLRLLAG LKELEEPFES HQIGSSAMPY KRNPMLSERI
CSLGRFLISL SQNGAYTHAT QWLERSLDDS ANRRLSLAES FLTADALLIL MEKVTKDLVV
NKAIIDKHIA EELPFMATEN ILMSAVKKGG DRQSLHEKIR IHSQAAADGI KQRGEPNHLL
ERIKADNEFG LTSEDISDLI DVKTFIGRSP EQVKEFIRTV KTQLEEFS
//
