ID V9H7L8_9CLOT Unreviewed; 476 AA.
AC V9H7L8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ORFNames=CSBG_01741 {ECO:0000313|EMBL:EEH98115.1};
OS Clostridium sp. 7_2_43FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=457396 {ECO:0000313|EMBL:EEH98115.1, ECO:0000313|Proteomes:UP000017809};
RN [1] {ECO:0000313|EMBL:EEH98115.1, ECO:0000313|Proteomes:UP000017809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_2_43FAA {ECO:0000313|EMBL:EEH98115.1,
RC ECO:0000313|Proteomes:UP000017809};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Strauss J.,
RA Ambrose C., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Clostridium sp. 7_2_43FAA.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEH98115.1}.
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DR EMBL; ACDK02000022; EEH98115.1; -; Genomic_DNA.
DR RefSeq; WP_008678440.1; NZ_JH815222.1.
DR AlphaFoldDB; V9H7L8; -.
DR STRING; 457396.CSBG_01741; -.
DR GeneID; 65398906; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_030949_1_1_9; -.
DR OrthoDB; 9768878at2; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000017809; Unassembled WGS sequence.
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:UP000017809}.
FT DOMAIN 369..453
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 476 AA; 54083 MW; E3D69DA4D524FC4D CRC64;
MKDLYNSPLN SRYASKEMSF IFSDDMKFST WRKLWVALAE GEKELGLNIT EEQIDELKSN
IYNINYDEAI KREKEVRHDV MSHVYAYGLQ CPSAKGIIHL GATSCYVGDN TDIIIMRDAL
LLIKKKVVTV LNHLSNFAIK YKDMPTLGFT HFQPAQLTTV GKRATLWMQD LVLDIENIEF
LLSTLKLRGV KGTTGTQASF MTLFNNDEEK VKELDSIVAK KMGFEKSYGV TGQTYPRKLD
SIVLNRLSEI AQSAYKFSND LRLLQSMKEI EEPFEKNQIG SSAMAYKRNP MRSERMGSLA
RYVIVNSLNP AITAATQWFE RTLDDSANKR IAVAEAFLAL DGVLNLYINI AENMVVYEKV
ISAHVNNELP FMATENIMME AVKRGGDRQE LHEKIRIHSM AAAQRVKGEG LDNDLIERII
KDDGFMLSEE EIRSIINPTK FVGRAPSQVV EFIEEYINPI IKVNKDALEV KSEITV
//
