ID A0A0G1UTX8_9BACT Unreviewed; 466 AA.
AC A0A0G1UTX8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:KKU61160.1};
GN ORFNames=UX85_C0004G0082 {ECO:0000313|EMBL:KKU61160.1};
OS Candidatus Beckwithbacteria bacterium GW2011_GWB1_47_15.
OC Bacteria; Candidatus Beckwithbacteria.
OX NCBI_TaxID=1618371 {ECO:0000313|EMBL:KKU61160.1, ECO:0000313|Proteomes:UP000033860};
RN [1] {ECO:0000313|EMBL:KKU61160.1, ECO:0000313|Proteomes:UP000033860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU61160.1}.
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DR EMBL; LCNT01000004; KKU61160.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1UTX8; -.
DR PATRIC; fig|1618371.3.peg.666; -.
DR Proteomes; UP000033860; 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:KKU61160.1}.
FT DOMAIN 24..337
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 356..443
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
SQ SEQUENCE 466 AA; 52062 MW; A6E4EF7B3D0CD886 CRC64;
MLYDGRVMAG KGAALVLPLS PLDGRYQEKV KELREYFSEE ALISYRVKVE VKYLLELVRF
LAPTFSGSPQ LPRRSRGDSA DLKSLSTESS KKLLHWSNNL SDKDVARVKK IEAKIRHDVK
AVEYVIGEKL TKMGLARLVP WVHWGLTSED TNNLSYGLMV VGAKEKVVLP AMRTLVDKLS
GLARVWAGTV MPARTHGQVA VPTTLGKEMA VFVSRFSWWL KKFAEVKPGG KLNGAVGNYN
AMVKIYPKKD WLGFSRKFVA GLGLTPTLIT TQIEPGTQLV YAFDLMRQFN NVGLNLAADL
WQYIAFDYLK QAAVKDEVGS STMPHKVNPI DFENAEGNLK LANGMLAVLA DKLPVSRLQR
DLSDSTVKRN IGVAWGYSLL AWKTLTDGLA KVAPNKNKLR QELEAHPEML AEAWQLSLRK
RGEAGAYEKV KDKTRGKPRE ELKEIKMWKA ADYVGLAEKL AKMRVG
//
