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Entry: E1UMY5_BACAS
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ID   E1UMY5_BACAS            Unreviewed;       430 AA.
AC   E1UMY5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   14-MAY-2014, entry version 24.
DE   SubName: Full=Adenylosuccinate lyase;
DE            EC=4.3.2.2;
GN   Name=purB; OrderedLocusNames=BAMF_0638;
OS   Bacillus amyloliquefaciens (strain ATCC 23350 / DSM 7 / BCRC 11601 /
OS   NBRC 15535 / NRRL B-14393).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=692420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM7;
RX   DOI=10.1099/ijs.0.023267-0 ;
RA   Borriss R., Chen X., Rueckert C., Blom J., Becker A., Baumgarth B.,
RA   Fan B., Pukall R., Schumann P., Sproer C., Junge H., Vater J.,
RA   Puhler A., Klenk H.P.;
RT   "Relationship of Bacillus amyloliquefaciens clades associated with
RT   strains DSM7T and FZB42: a proposal for Bacillus amyloliquefaciens
RT   subsp. amyloliquefaciens subsp. nov. and Bacillus amyloliquefaciens
RT   subsp. plantarum subsp. nov. based on their discriminating complete
RT   genome sequences.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23350 / DSM 7 / BCRC 11601 / NBRC 15535 / NRRL B-14393;
RX   PubMed=21262282; DOI=10.1016/j.jbiotec.2011.01.006;
RA   Ruckert C., Blom J., Chen X., Reva O., Borriss R.;
RT   "Genome sequence of B. amyloliquefaciens type strain DSM7(T) reveals
RT   differences to plant-associated B. amyloliquefaciens FZB42.";
RL   J. Biotechnol. 155:78-85(2011).
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DR   EMBL; FN597644; CBI41764.1; -; Genomic_DNA.
DR   RefSeq; YP_003919234.1; NC_014551.1.
DR   ProteinModelPortal; E1UMY5; -.
DR   EnsemblBacteria; CBI41764; CBI41764; BAMF_0638.
DR   GeneID; 9779589; -.
DR   KEGG; bao:BAMF_0638; -.
DR   PATRIC; 42470167; VBIBacAmy172706_0684.
DR   HOGENOM; HOG000033912; -.
DR   KO; K01756; -.
DR   BioCyc; BAMY692420:GHU2-703-MONOMER; -.
DR   GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-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:0009152; P:purine ribonucleotide biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.275.10; -; 1.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
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   PANTHER; PTHR11444; PTHR11444; 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; SSF48557; 1.
DR   TIGRFAMs; TIGR00928; purB; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   4: Predicted;
KW   Complete proteome; Lyase.
SQ   SEQUENCE   430 AA;  49421 MW;  46C08B4235A5EB1F CRC64;
     MIERYSRPEM SAIWTDENRY QAWLEVEILA CEAWAELGVI PKEDVKVMRE NASFDINRIL
     EIEQDTRHDV VAFTRAVSES LGEERKWVHY GLTSTDVVDT ALSYLLKQAN EILLKDIERF
     VDIIKEKAKE HKYTVMMGRT HGVHAEPTTF GLKLALWHEE MKRNLERFKQ AKEGIEVGKL
     SGAVGTYANI DPFVEQYVCE KLGLKAAPIS TQTLQRDRHA DYMAALALIA TSIEKFAVEI
     RGLQKSETRE VEEFFAKGQK GSSAMPHKRN PIGSENMTGM ARVIRGYMLT AYENVPLWHE
     RDISHSSAER IILPDATTAL NFMLNRFSNI VKNLTVFPEN MKRNMDRTLG LIYSQRVLLA
     LIDTGLPREE AYDTVQPKAM EAWEKQVPFR QLVEAEEKIT SRLTPEQIAD CFDYNYHLKN
     VDLIFDRLGL
//
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