ID A0A0U3R073_9ACTN Unreviewed; 419 AA.
AC A0A0U3R073;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:ALV38297.1};
GN ORFNames=AS200_01360 {ECO:0000313|EMBL:ALV38297.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV38297.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV38297.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV38297.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP013743; ALV38297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3R073; -.
DR STRING; 1725411.AS200_01360; -.
DR KEGG; scx:AS200_01360; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000068029; Chromosome.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate 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 CDD; cd01360; Adenylsuccinate_lyase_1; 1.
DR Gene3D; 1.10.275.60; -; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR InterPro; IPR019468; AdenyloSucc_lyase_C.
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 NCBIfam; TIGR00928; purB; 1.
DR PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43172:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SMART; SM00998; ADSL_C; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ALV38297.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT DOMAIN 341..412
FT /note="Adenylosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00998"
SQ SEQUENCE 419 AA; 45790 MW; 957030BD65DDB677 CRC64;
MAGLFTDSSR YATWVRVEIL ASEAQAALGH VPHEAVADMR RARVPAPERV AALERERDHE
VLSFLAAYCE GIPDSSARFV HLGMTSYDLV DTALGHTLTR ATDLLTTAAR RLRRILTGRA
LEHWDTVMVG RTHGMHAEPT TFGHKLAGHA FAVDRCLHRL AAARQAVAVG TISGSVGTYA
LIDPRVEDHV CTALGLTAEP APSQVVARDR HAQLLQAVAT LGACIEHLAL ELRLLQRTEV
REVEEARTSA YQGSSAMPHK RNPTTSERLC GLARLLRGYA DTALENVALW HERDLAHQSV
ERVILPDSLC VGHFQATRAG DLVAALTVDA DRMRAHIDHT DGLIYSSSVL AELLGEGMER
EHAYRSVQAA ANHTLATGEH FAASLAKEGI DLAGLGPERF LSHHDVIRTR LEKLHELQD
//
