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Adenylosuccinate lyase (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) (Glutamyl--tRNA ligase regulatory factor)

 PUR8_BACSU              Reviewed;         431 AA.
P12047;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
07-JUN-2017, entry version 148.
RecName: Full=Adenylosuccinate lyase;
Short=ASL;
EC=4.3.2.2;
AltName: Full=Adenylosuccinase;
Short=ASase;
AltName: Full=Glutamyl--tRNA ligase regulatory factor;
Name=purB; Synonyms=purE; OrderedLocusNames=BSU06440;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3036807;
Ebbole D.J., Zalkin H.;
"Cloning and characterization of a 12-gene cluster from Bacillus
subtilis encoding nine enzymes for de novo purine nucleotide
synthesis.";
J. Biol. Chem. 262:8274-8287(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
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.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
PROTEIN SEQUENCE OF 1-30.
STRAIN=168 / BGSC1A1;
PubMed=1608947; DOI=10.1073/pnas.89.12.5389;
Gendron N., Breton R., Champagne N., Lapointe J.;
"Adenylosuccinate lyase of Bacillus subtilis regulates the activity of
the glutamyl-tRNA synthetase.";
Proc. Natl. Acad. Sci. U.S.A. 89:5389-5392(1992).
[4]
CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF HIS-89; HIS-141;
GLN-212; ASN-270 AND ARG-301.
PubMed=15182182; DOI=10.1021/bi0494774;
Segall M.L., Colman R.F.;
"Gln212, Asn270, and Arg301 are critical for catalysis by
adenylosuccinate lyase from Bacillus subtilis.";
Biochemistry 43:7391-7402(2004).
[5]
SUBUNIT.
PubMed=18237141; DOI=10.1021/bi701400c;
De Zoysa Ariyananda L., Colman R.F.;
"Evaluation of types of interactions in subunit association in
Bacillus subtilis adenylosuccinate lyase.";
Biochemistry 47:2923-2934(2008).
[6]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).
PubMed=10926519; DOI=10.1006/jmbi.2000.3970;
Toth E.A., Worby C., Dixon J.E., Goedken E.R., Marqusee S.,
Yeates T.O.;
"The crystal structure of adenylosuccinate lyase from Pyrobaculum
aerophilum reveals an intracellular protein with three disulfide
bonds.";
J. Mol. Biol. 301:433-450(2000).
-!- FUNCTION: Influences the affinity of glutamyl--tRNA ligase for its
substrates and increases its thermostability.
-!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
{ECO:0000269|PubMed:15182182}.
-!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D-
ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-
(5-phospho-D-ribosyl)imidazole-4-carboxamide.
{ECO:0000269|PubMed:15182182}.
-!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
AMP from IMP: step 2/2.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
-!- SUBUNIT: Homotetramer. Residues from neighboring subunits
contribute catalytic and substrate-binding residues to each active
site. {ECO:0000269|PubMed:15182182, ECO:0000269|PubMed:18237141}.
-!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J02732; AAA22676.1; -; Genomic_DNA.
EMBL; AL009126; CAB12464.1; -; Genomic_DNA.
PIR; C29326; WZBSDS.
RefSeq; NP_388526.1; NC_000964.3.
RefSeq; WP_003233955.1; NZ_JNCM01000032.1.
PDB; 1F1O; X-ray; 3.25 A; A=1-431.
PDBsum; 1F1O; -.
ProteinModelPortal; P12047; -.
SMR; P12047; -.
IntAct; P12047; 3.
MINT; MINT-8364879; -.
STRING; 224308.Bsubs1_010100003638; -.
PaxDb; P12047; -.
PRIDE; P12047; -.
EnsemblBacteria; CAB12464; CAB12464; BSU06440.
GeneID; 936048; -.
KEGG; bsu:BSU06440; -.
PATRIC; fig|224308.179.peg.700; -.
eggNOG; ENOG4105C83; Bacteria.
eggNOG; COG0015; LUCA.
HOGENOM; HOG000033912; -.
InParanoid; P12047; -.
KO; K01756; -.
OMA; ASSCEKI; -.
PhylomeDB; P12047; -.
BioCyc; BSUB:BSU06440-MONOMER; -.
BRENDA; 4.3.2.2; 658.
SABIO-RK; P12047; -.
UniPathway; UPA00074; UER00132.
UniPathway; UPA00075; UER00336.
EvolutionaryTrace; P12047; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IBA:GO_Central.
GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IDA:MGI.
GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006167; P:AMP biosynthetic process; IDA:MGI.
Gene3D; 1.10.275.10; -; 1.
InterPro; IPR019468; AdenyloSucc_lyase_C.
InterPro; IPR024083; Fumarase/histidase_N.
InterPro; IPR020557; Fumarate_lyase_CS.
InterPro; IPR000362; Fumarate_lyase_fam.
InterPro; IPR022761; Fumarate_lyase_N.
InterPro; IPR008948; L-Aspartase-like.
InterPro; IPR004769; Pur_lyase.
Pfam; PF10397; ADSL_C; 1.
Pfam; PF00206; Lyase_1; 1.
PRINTS; PR00149; FUMRATELYASE.
SMART; SM00998; ADSL_C; 1.
SUPFAM; SSF48557; SSF48557; 1.
TIGRFAMs; TIGR00928; purB; 1.
PROSITE; PS00163; FUMARATE_LYASES; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing; Lyase;
Purine biosynthesis; Reference proteome.
CHAIN 1 431 Adenylosuccinate lyase.
/FTId=PRO_0000137873.
REGION 4 5 Substrate binding. {ECO:0000250}.
REGION 67 69 Substrate binding. {ECO:0000250}.
REGION 93 94 Substrate binding. {ECO:0000250}.
REGION 268 270 Substrate binding. {ECO:0000250}.
ACT_SITE 141 141 Proton donor/acceptor. {ECO:0000250}.
ACT_SITE 262 262 Proton donor/acceptor. {ECO:0000250}.
BINDING 212 212 Substrate. {ECO:0000250}.
BINDING 276 276 Substrate. {ECO:0000250}.
BINDING 301 301 Substrate. {ECO:0000250}.
BINDING 306 306 Substrate. {ECO:0000250}.
MUTAGEN 89 89 H->Q: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
MUTAGEN 141 141 H->Q: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
MUTAGEN 212 212 Q->E: Decreases catalytic activity 1000-
fold. {ECO:0000269|PubMed:15182182}.
MUTAGEN 212 212 Q->M: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
MUTAGEN 270 270 N->D,L: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
MUTAGEN 301 301 R->K,Q: Abolishes enzyme activity.
{ECO:0000269|PubMed:15182182}.
CONFLICT 5 5 Y -> K (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 431 AA; 49485 MW; 89D2ED7F7F6D46A2 CRC64;
MIERYSRPEM SAIWTDENRF QAWLEVEILA CEAWAELGVI PKEDVKVMRE NASFDINRIL
EIEKDTRHDV VAFTRAVSES LGEERKWVHY GLTSTDVVDT ALSYLLKQAN DILLKDLERF
VDIIKEKAKE HKYTVMMGRT HGVHAEPTTF GLKLALWHEE MKRNLERFKQ AKAGIEVGKI
SGAVGTYANI DPFVEQYVCE KLGLKAAPIS TQTLQRDRHA DYMATLALIA TSIEKFAVEI
RGLQKSETRE VEEFFAKGQK GSSAMPHKRN PIGSENMTGM ARVIRGYMMT AYENVPLWHE
RDISHSSAER IILPDATIAL NYMLNRFSNI VKNLTVFPEN MKRNMDRTLG LIYSQRVLLA
LIDTGLTREE AYDTVQPKAM EAWEKQVPFR ELVEAEEKIT SRLSPEKIAD CFDYNYHLKN
VDLIFERLGL A


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