PUR8_VIBC3
ID PUR8_VIBC3 Reviewed; 456 AA.
AC A0A0H3AL67;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Adenylosuccinate lyase;
DE Short=ASL;
DE EC=4.3.2.2 {ECO:0000250|UniProtKB:P0AB89};
DE AltName: Full=Adenylosuccinase;
GN Name=purB {ECO:0000312|EMBL:ABQ21474.1};
GN OrderedLocusNames=VC0395_A0644 {ECO:0000312|EMBL:ABQ21474.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION (MICROBIAL INFECTION), CATALYTIC ACTIVITY (MICROBIAL INFECTION),
RP AND DISRUPTION PHENOTYPE.
RX PubMed=33926955; DOI=10.1126/science.abe6494;
RA Sleiman D., Garcia P.S., Lagune M., Loc'h J., Haouz A., Taib N.,
RA Roethlisberger P., Gribaldo S., Marliere P., Kaminski P.A.;
RT "A third purine biosynthetic pathway encoded by aminoadenine-based viral
RT DNA genomes.";
RL Science 372:516-520(2021).
CC -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC and fumarate. {ECO:0000250|UniProtKB:P0AB89}.
CC -!- FUNCTION: (Microbial infection) Catalyzes the conversion of 2-amino-2'-
CC deoxyadenylo-succinate to dZMP and fumarate, when the bacterium is
CC infected by a phage that produces the substrate of this reaction, a
CC step in the synthesis of dZTP (2-amino-2'-deoxyadenosine 5'-
CC triphosphate), which is a nucleotide then used by the phage as a DNA
CC polymerase substrate. {ECO:0000269|PubMed:33926955}.
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:0000250|UniProtKB:P0AB89};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854;
CC Evidence={ECO:0000250|UniProtKB:P0AB89};
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:0000250|UniProtKB:P0AB89};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23921;
CC Evidence={ECO:0000250|UniProtKB:P0AB89};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-amino-2'-deoxyadenylo-succinate = dZMP + fumarate;
CC Xref=Rhea:RHEA:67636, ChEBI:CHEBI:29806, ChEBI:CHEBI:172924,
CC ChEBI:CHEBI:172927; Evidence={ECO:0000269|PubMed:33926955};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67637;
CC Evidence={ECO:0000305|PubMed:33926955};
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 2/2. {ECO:0000250|UniProtKB:P0AB89}.
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:0000250|UniProtKB:P0AB89}.
CC -!- PATHWAY: Purine metabolism. {ECO:0000269|PubMed:33926955}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0AB89}.
CC -!- DISRUPTION PHENOTYPE: A reduction in the expression of purB leads to a
CC reduction in the efficiency of infection by a Vibrio phage.
CC {ECO:0000269|PubMed:33926955}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000305}.
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DR EMBL; CP000627; ABQ21474.1; -; Genomic_DNA.
DR RefSeq; WP_000423489.1; NZ_JAACZH010000005.1.
DR SMR; A0A0H3AL67; -.
DR STRING; 345073.VC395_1141; -.
DR EnsemblBacteria; ABQ21474; ABQ21474; VC0395_A0644.
DR KEGG; vco:VC0395_A0644; -.
DR PATRIC; fig|345073.21.peg.1108; -.
DR eggNOG; COG0015; Bacteria.
DR OMA; TQVNPCD; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000000249; Chromosome 2.
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 Gene3D; 1.10.275.10; -; 1.
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 InterPro; IPR013539; PurB_C.
DR Pfam; PF08328; ASL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00928; purB; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW Lyase; Purine biosynthesis.
FT CHAIN 1..456
FT /note="Adenylosuccinate lyase"
FT /id="PRO_0000453795"
FT ACT_SITE 171
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT ACT_SITE 296
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 15..16
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 90..92
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 122..123
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 248
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 297
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 302..304
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 310
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 336
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
FT BINDING 341..345
FT /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT /ligand_id="ChEBI:CHEBI:57567"
FT /evidence="ECO:0000250|UniProtKB:P0AB89"
SQ SEQUENCE 456 AA; 51335 MW; 1B57F9A5A1FDD859 CRC64;
MELSALTAVS PVDGRYGSKT IALRSIFSEF GLLKYRTIVE IRWLQKLAAT AEIAEVPAFS
AEANQFLDAI AANFNEADAL RIKEIERTTN HDVKAVEYFL KEKVAAMPEL HAVNEFIHFA
CTSEDINNTS HALMLKEARD TVILPEIRNV IDAIRKLAEE YRDIPLLSRT HGQPASPSTM
GKEMANVAYR MERQYKQIAN VEILAKINGA VGNYNAHLSA YPTVDWHKFS EEFITESLGV
DWNPYTTQIE PHDYIAELFE AVARFNTILI DFDRDVWGYI ALGHFKQRTI AGEIGSSTMP
HKVNPIDFEN SEGNLGLANA VFTHLAQKLP ISRWQRDLTD STVLRNLGVG VGYAIIAYTS
TLKGISKLEV NRDALLAELD HNWEVLAEPI QTVMRRYGIE KPYEKLKELT RGKRVDGEAM
RQFIDGLALP AEEKTRLKAM TPASYIGYAI ELTDKL
