ID A0A160KPT9_9MICO Unreviewed; 460 AA.
AC A0A160KPT9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:AND15432.1};
GN ORFNames=A6122_0271 {ECO:0000313|EMBL:AND15432.1}, C5C18_06960
GN {ECO:0000313|EMBL:PPG07537.1};
OS Rathayibacter tritici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=33888 {ECO:0000313|EMBL:AND15432.1, ECO:0000313|Proteomes:UP000077071};
RN [1] {ECO:0000313|EMBL:AND15432.1, ECO:0000313|Proteomes:UP000077071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND15432.1,
RC ECO:0000313|Proteomes:UP000077071};
RA Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PPG07537.1, ECO:0000313|Proteomes:UP000239776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSPB 2748 {ECO:0000313|EMBL:PPG07537.1,
RC ECO:0000313|Proteomes:UP000239776};
RA Davis E.W.II., Tabima J.F., Weisberg A.J., Lopes L.D., Wiseman M.S.,
RA Wiseman M.S., Pupko T., Belcher M.S., Sechler A.J., Tancos M.A.,
RA Schroeder B.K., Murray T.D., Luster D.G., Schneider W.L., Rogers E.,
RA Andreote F.D., Grunwald N.J., Putnam M.L., Chang J.H.;
RT "Bacteriophage NCPPB3778 and a type I-E CRISPR drive the evolution of the
RT US Biological Select Agent, Rathayibacter toxicus.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC and fumarate. {ECO:0000256|ARBA:ARBA00025012}.
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DR EMBL; CP015515; AND15432.1; -; Genomic_DNA.
DR EMBL; PSUO01000008; PPG07537.1; -; Genomic_DNA.
DR RefSeq; WP_068250696.1; NZ_PSWT01000029.1.
DR AlphaFoldDB; A0A160KPT9; -.
DR STRING; 33888.A6122_0271; -.
DR KEGG; rtn:A6122_0271; -.
DR PATRIC; fig|33888.3.peg.315; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000077071; Chromosome.
DR Proteomes; UP000239776; Unassembled WGS sequence.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:InterPro.
DR GO; GO:0006188; P:IMP biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
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; IPR047136; PurB_bact.
DR InterPro; IPR013539; PurB_C.
DR PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF08328; ASL_C; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AND15432.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077071}.
FT DOMAIN 14..308
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 329..449
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
SQ SEQUENCE 460 AA; 50404 MW; F264B0ABDB79349A CRC64;
MTSLPTQPLS PLDGRYSGAV SSLGEYLSEA GLNRARVHVE VEWLLALTDR RLFGSEPVDA
ATAEELRRRA RDFGQPEIDE LAALEARTRH DVKAVEYLVR RWLDDLGLER IAELTHFAAT
SEDINNLSYA IVVRRAVGEI WLPKLRSVVD SLRELAVRYR DESMLSRTHG QPATPTTMGK
EFAVYAYRLE RVIAQIEATD YLGKFSGATG TFAAHLAADP GTDWPALAEQ FVTSLGLVFT
PLTTQIESHD WQAELYGRAA HANRILHNIC TDVWTYISLG YFRQIPQAGA TGSSTMPHKI
NPIRFENAEA NLELSSALLD SLAQTLVTSR LQRDLTDSTT QRNIGVAFGH SLLALDNIAR
GLLEIDLDPT ALAADLDGNW EVLAEAIQTV IRAEVAAGRS SITDPYALLK DLTRGKRLGA
DDLAVFVQGL DIGDAAKERL LALTPASYTG LASALVDRLG
//
