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Database: UniProt/TrEMBL
Entry: B7GFT4_ANOFW
LinkDB: B7GFT4_ANOFW
Original site: B7GFT4_ANOFW 
ID   B7GFT4_ANOFW            Unreviewed;       439 AA.
AC   B7GFT4;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   29-OCT-2014, entry version 38.
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   Name=purB {ECO:0000313|EMBL:ACJ32614.1};
GN   OrderedLocusNames=Aflv_0230 {ECO:0000313|EMBL:ACJ32614.1};
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915 {ECO:0000313|EMBL:ACJ32614.1, ECO:0000313|Proteomes:UP000000742};
RN   [1] {ECO:0000313|EMBL:ACJ32614.1, ECO:0000313|Proteomes:UP000000742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1 {ECO:0000313|Proteomes:UP000000742};
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L.,
RA   Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
CC   -!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D-
CC       ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-
CC       (5-phospho-D-ribosyl)imidazole-4-carboxamide.
CC       {ECO:0000256|RuleBase:RU361172}.
CC   -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP.
CC       {ECO:0000256|RuleBase:RU361172}.
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway;
CC       AMP from IMP: step 2/2. {ECO:0000256|RuleBase:RU361172}.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-
CC       amino-1-(5-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}.
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DR   EMBL; CP000922; ACJ32614.1; -; Genomic_DNA.
DR   RefSeq; YP_002314599.1; NC_011567.1.
DR   ProteinModelPortal; B7GFT4; -.
DR   STRING; 491915.Aflv_0230; -.
DR   EnsemblBacteria; ACJ32614; ACJ32614; Aflv_0230.
DR   GeneID; 7036462; -.
DR   KEGG; afl:Aflv_0230; -.
DR   PATRIC; 20952199; VBIAnoFla45531_0236.
DR   eggNOG; COG0015; -.
DR   HOGENOM; HOG000033912; -.
DR   KO; K01756; -.
DR   OMA; RNMGSTF; -.
DR   OrthoDB; EOG686NDB; -.
DR   BioCyc; AFLA491915:GHEO-280-MONOMER; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
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: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; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000742};
KW   Lyase {ECO:0000256|RuleBase:RU361172, ECO:0000313|EMBL:ACJ32614.1};
KW   Purine biosynthesis {ECO:0000256|RuleBase:RU361172};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000742}.
SQ   SEQUENCE   439 AA;  50644 MW;  E10BEF19279DEBAC CRC64;
     MDRSEDERMI ERYTRPEMGA IWTEENRFRA WLEVEILACE AWAELGVIPK EDVEKIRQHA
     SFDIDRIKQI EEETRHDVVA FTRAVSETLG EERKWVHYGL TSTDVVDTAL SYLLKQANEI
     LLRDLENLIA VLKEKAIEHK YTVMMGRTHG VHAEPTTFGL KLALWYAEME RNLERFKQAA
     ETVRVGKISG AVGTYANIDP FVEQYVCEKL GLQPAPISTQ TLQRDRHAHY MATLALIATS
     IEKFAVEIRG LQKSETREVE EFFAKGQKGS SAMPHKRNPI GSENMTGMAR VIRGYMLTAY
     ENVPLWHERD ISHSSAERII LPDATIALDY MLNRFTNIVK NLTVFPENMK KNMDRTLGLI
     YSQRVLLALI DTGMTREEAY DLVQPKAMEA WEKQVPFRSL IEADEVITSR LTKDQIADCF
     DYNYHLKHVD TIFRRLGLQ
//
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