ID A0A0H3J4Y1_CLOPA Unreviewed; 476 AA.
AC A0A0H3J4Y1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:AJA52075.1};
GN ORFNames=CLPA_c20170 {ECO:0000313|EMBL:AJA52075.1}, CP6013_01162
GN {ECO:0000313|EMBL:KRU11915.1};
OS Clostridium pasteurianum DSM 525 = ATCC 6013.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262449 {ECO:0000313|EMBL:AJA52075.1, ECO:0000313|Proteomes:UP000030905};
RN [1] {ECO:0000313|EMBL:AJA52075.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 525 {ECO:0000313|EMBL:AJA52075.1};
RX PubMed=25700415;
RA Poehlein A., Grosse-Honebrink A., Zhang Y., Minton N.P., Daniel R.;
RT "Complete Genome Sequence of the Nitrogen-Fixing and Solvent-Producing
RT Clostridium pasteurianum DSM 525.";
RL Genome Announc. 3:e01591-e01514(2015).
RN [2] {ECO:0000313|EMBL:KRU11915.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU11915.1};
RA Pyne M.E., Utturkar S.M., Brown S.D., Moo-Young M., Chung D.A., Chou P.C.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KRU11915.1, ECO:0000313|Proteomes:UP000028042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6013 {ECO:0000313|EMBL:KRU11915.1,
RC ECO:0000313|Proteomes:UP000028042};
RX PubMed=25103768;
RA Pyne M.E., Utturkar S., Brown S.D., Moo-Young M., Chung D.A., Chou C.P.;
RT "Improved Draft Genome Sequence of Clostridium pasteurianum Strain ATCC
RT 6013 (DSM 525) Using a Hybrid Next-Generation Sequencing Approach.";
RL Genome Announc. 2:0-0(0).
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; CP009268; AJA52075.1; -; Genomic_DNA.
DR EMBL; JPGY02000001; KRU11915.1; -; Genomic_DNA.
DR RefSeq; WP_003442300.1; NZ_JPGY02000001.1.
DR AlphaFoldDB; A0A0H3J4Y1; -.
DR GeneID; 76626422; -.
DR KEGG; cpae:CPAST_c20170; -.
DR KEGG; cpat:CLPA_c20170; -.
DR PATRIC; fig|1262449.3.peg.978; -.
DR eggNOG; COG0015; Bacteria.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000028042; Unassembled WGS sequence.
DR Proteomes; UP000030905; 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 GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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 Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361172};
KW Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW Reference proteome {ECO:0000313|Proteomes:UP000030905}.
FT DOMAIN 369..453
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 476 AA; 54271 MW; 517DEFAE1C943E52 CRC64;
MRNIYQTPLN TRYASKDMSY LFSDEMKFKT WRKLWVALAE SEKELGLNIT DEQIEELKSH
IDDINYEVAE KREKEVRHDV MSHVYAYGVQ CPKAKGIIHL GATSCYVGDN TDIIIMKKAL
ILIKNKIINV IEHLSEFALK YKDLPALGYT HLQPAQLTTV GKRATLWMQD LFLDLENINF
VIDTIKLRGV KGTTGTQASF MELFDCNEEK IKKLEKKVTE RMGFKEAYAV TGQTYSRKVD
SIVLNTLSEI AQSAYKFSND LRILQSFKEI EEPFEAHQIG SSAMAYKRNP MRSERIGSLA
RYVIVNSLNP AVTAATQWFE RTLDDSANKR ISIAEAFLAL DGVLNLYINV SSNLVVYDKV
IAARVNNELP FMATENILME AVKRGGDRQE LHEKIRVYSM ETAKRVKQDG LDNNLIDLIA
KDPAFNIKKE EILSILDAKN FVGRAPGQVT DFIKDYVEPI LESNREILDI NVDINV
//
