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Protein

Adenylosuccinate lyase

Gene

purB

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Influences the affinity of glutamyl--tRNA ligase for its substrates and increases its thermostability.

Catalytic activityi

N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.1 Publication
(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.1 Publication

Pathwayi: AMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes AMP from IMP.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Adenylosuccinate synthetase (purA)
  2. Adenylosuccinate lyase (purB)
This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoribosylaminoimidazole-succinocarboxamide synthase (purC)
  2. Adenylosuccinate lyase (purB)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei141 – 1411Proton donor/acceptorBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Active sitei262 – 2621Proton donor/acceptorBy similarity
Binding sitei276 – 2761SubstrateBy similarity
Binding sitei301 – 3011SubstrateBy similarity
Binding sitei306 – 3061SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU06440-MONOMER.
RETL1328306-WGS:GSTH-2282-MONOMER.
BRENDAi4.3.2.2. 658.
SABIO-RKP12047.
UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylosuccinate lyase (EC:4.3.2.2)
Short name:
ASL
Alternative name(s):
Adenylosuccinase
Short name:
ASase
Glutamyl--tRNA ligase regulatory factor
Gene namesi
Name:purB
Synonyms:purE
Ordered Locus Names:BSU06440
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891H → Q: Abolishes enzyme activity. 1 Publication
Mutagenesisi141 – 1411H → Q: Abolishes enzyme activity. 1 Publication
Mutagenesisi212 – 2121Q → E: Decreases catalytic activity 1000-fold. 1 Publication
Mutagenesisi212 – 2121Q → M: Abolishes enzyme activity. 1 Publication
Mutagenesisi270 – 2701N → D or L: Abolishes enzyme activity. 1 Publication
Mutagenesisi301 – 3011R → K or Q: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Adenylosuccinate lyasePRO_0000137873Add
BLAST

Proteomic databases

PaxDbiP12047.
PRIDEiP12047.

Interactioni

Subunit structurei

Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site.2 Publications

Protein-protein interaction databases

IntActiP12047. 3 interactions.
MINTiMINT-8364879.
STRINGi224308.Bsubs1_010100003638.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F1OX-ray3.25A1-431[»]
ProteinModelPortaliP12047.
SMRiP12047. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12047.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 52Substrate bindingBy similarity
Regioni67 – 693Substrate bindingBy similarity
Regioni93 – 942Substrate bindingBy similarity
Regioni268 – 2703Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
InParanoidiP12047.
KOiK01756.
OMAiVQENAMK.
OrthoDBiEOG686NDB.
PhylomeDBiP12047.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12047-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIERYSRPEM SAIWTDENRF QAWLEVEILA CEAWAELGVI PKEDVKVMRE
60 70 80 90 100
NASFDINRIL EIEKDTRHDV VAFTRAVSES LGEERKWVHY GLTSTDVVDT
110 120 130 140 150
ALSYLLKQAN DILLKDLERF VDIIKEKAKE HKYTVMMGRT HGVHAEPTTF
160 170 180 190 200
GLKLALWHEE MKRNLERFKQ AKAGIEVGKI SGAVGTYANI DPFVEQYVCE
210 220 230 240 250
KLGLKAAPIS TQTLQRDRHA DYMATLALIA TSIEKFAVEI RGLQKSETRE
260 270 280 290 300
VEEFFAKGQK GSSAMPHKRN PIGSENMTGM ARVIRGYMMT AYENVPLWHE
310 320 330 340 350
RDISHSSAER IILPDATIAL NYMLNRFSNI VKNLTVFPEN MKRNMDRTLG
360 370 380 390 400
LIYSQRVLLA LIDTGLTREE AYDTVQPKAM EAWEKQVPFR ELVEAEEKIT
410 420 430
SRLSPEKIAD CFDYNYHLKN VDLIFERLGL A
Length:431
Mass (Da):49,485
Last modified:October 1, 1989 - v1
Checksum:i89D2ED7F7F6D46A2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51Y → K AA sequence (PubMed:1608947).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02732 Genomic DNA. Translation: AAA22676.1.
AL009126 Genomic DNA. Translation: CAB12464.1.
PIRiC29326. WZBSDS.
RefSeqiNP_388526.1. NC_000964.3.
WP_003233955.1. NZ_JNCM01000032.1.

Genome annotation databases

EnsemblBacteriaiCAB12464; CAB12464; BSU06440.
GeneIDi936048.
KEGGibsu:BSU06440.
PATRICi18972930. VBIBacSub10457_0679.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02732 Genomic DNA. Translation: AAA22676.1.
AL009126 Genomic DNA. Translation: CAB12464.1.
PIRiC29326. WZBSDS.
RefSeqiNP_388526.1. NC_000964.3.
WP_003233955.1. NZ_JNCM01000032.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F1OX-ray3.25A1-431[»]
ProteinModelPortaliP12047.
SMRiP12047. Positions 2-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP12047. 3 interactions.
MINTiMINT-8364879.
STRINGi224308.Bsubs1_010100003638.

Proteomic databases

PaxDbiP12047.
PRIDEiP12047.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12464; CAB12464; BSU06440.
GeneIDi936048.
KEGGibsu:BSU06440.
PATRICi18972930. VBIBacSub10457_0679.

Phylogenomic databases

eggNOGiENOG4105C83. Bacteria.
COG0015. LUCA.
HOGENOMiHOG000033912.
InParanoidiP12047.
KOiK01756.
OMAiVQENAMK.
OrthoDBiEOG686NDB.
PhylomeDBiP12047.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00132.
UPA00075; UER00336.
BioCyciBSUB:BSU06440-MONOMER.
RETL1328306-WGS:GSTH-2282-MONOMER.
BRENDAi4.3.2.2. 658.
SABIO-RKP12047.

Miscellaneous databases

EvolutionaryTraceiP12047.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
InterProiIPR019468. AdenyloSucc_lyase_C.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
IPR004769. Pur_lyase.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10397. ADSL_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SMARTiSM00998. ADSL_C. 1 hit.
[Graphical view]
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00928. purB. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis."
    Ebbole D.J., Zalkin H.
    J. Biol. Chem. 262:8274-8287(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Adenylosuccinate lyase of Bacillus subtilis regulates the activity of the glutamyl-tRNA synthetase."
    Gendron N., Breton R., Champagne N., Lapointe J.
    Proc. Natl. Acad. Sci. U.S.A. 89:5389-5392(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-30.
    Strain: 168 / BGSC1A1.
  4. "Gln212, Asn270, and Arg301 are critical for catalysis by adenylosuccinate lyase from Bacillus subtilis."
    Segall M.L., Colman R.F.
    Biochemistry 43:7391-7402(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF HIS-89; HIS-141; GLN-212; ASN-270 AND ARG-301.
  5. "Evaluation of types of interactions in subunit association in Bacillus subtilis adenylosuccinate lyase."
    De Zoysa Ariyananda L., Colman R.F.
    Biochemistry 47:2923-2934(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds."
    Toth E.A., Worby C., Dixon J.E., Goedken E.R., Marqusee S., Yeates T.O.
    J. Mol. Biol. 301:433-450(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).

Entry informationi

Entry nameiPUR8_BACSU
AccessioniPrimary (citable) accession number: P12047
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: February 17, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.