ID A4AET7_9ACTN Unreviewed; 463 AA.
AC A4AET7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:EAR26138.1};
DE EC=4.3.2.2 {ECO:0000313|EMBL:EAR26138.1};
GN ORFNames=A20C1_09664 {ECO:0000313|EMBL:EAR26138.1};
OS marine actinobacterium PHSC20C1.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=312284 {ECO:0000313|EMBL:EAR26138.1, ECO:0000313|Proteomes:UP000003868};
RN [1] {ECO:0000313|EMBL:EAR26138.1, ECO:0000313|Proteomes:UP000003868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHSC20C1 {ECO:0000313|EMBL:EAR26138.1,
RC ECO:0000313|Proteomes:UP000003868};
RA Murray A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAR26138.1}.
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DR EMBL; AAOB01000001; EAR26138.1; -; Genomic_DNA.
DR AlphaFoldDB; A4AET7; -.
DR STRING; 312284.A20C1_09664; -.
DR eggNOG; COG0015; Bacteria.
DR HOGENOM; CLU_025566_2_0_11; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000003868; Unassembled WGS sequence.
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: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:EAR26138.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003868}.
FT DOMAIN 18..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 463 AA; 50850 MW; A2CC9D4331CBF421 CRC64;
MSPLPVQPLS PLDGRYRPAV SALGEYLSEA GLNRARVHVE VEWLIFLTGK SLFGSSPLTA
DQITALRTFA TDFGQEQIDE LARLEATTRH DVKAVEYLVR AKLDELGLNG IAELTHFAAT
SEDINNLSYA LTISDAVREV WLPKFRIVLD ALRAQSELMR DDAMLAHTHG QPATPTTMGK
EFAVFVYRLD RILTRIEGIS YLGKFSGATG TFAAHLAADP DQNWPALSKE FVESLGLDWN
PLTTQIESHD WQVELYQATS HANRVLHNLC TDVWSYISMG YFRQIPQAGA TGSSTMPHKI
NPIRFENAEA NLELSSALLE SLAQTLVTSR LQRDLTDSTT QRNVGVAYGH SLLALDNIER
GLREIALNPV ALDADLDSNW EILGEAIQTV IRAEVTAGRS TISDPYAILK ELTRGKRINA
TDLSEFIAGL DIGADAKARL QALTPATYVG LASSLVDYLG DSK
//
