ID B7GFT4_ANOFW Unreviewed; 439 AA.
AC B7GFT4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 07-SEP-2016, entry version 52.
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 ProteinModelPortal; B7GFT4; -.
DR STRING; 491915.Aflv_0230; -.
DR EnsemblBacteria; ACJ32614; ACJ32614; Aflv_0230.
DR KEGG; afl:Aflv_0230; -.
DR PATRIC; 20952199; VBIAnoFla45531_0236.
DR eggNOG; ENOG4105C83; Bacteria.
DR eggNOG; COG0015; LUCA.
DR HOGENOM; HOG000033912; -.
DR KO; K01756; -.
DR OMA; VQENAMK; -.
DR OrthoDB; POG091H0168; -.
DR BioCyc; AFLA491915:GHEO-280-MONOMER; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000000742; Chromosome.
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}.
FT DOMAIN 357 437 ADSL_C. {ECO:0000259|SMART:SM00998}.
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
//
