ID A0A094PRP4_9ACTN Unreviewed; 462 AA.
AC A0A094PRP4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:KGA04661.1};
GN ORFNames=GM43_3895 {ECO:0000313|EMBL:KGA04661.1};
OS actinobacterium acMicro-4.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504317 {ECO:0000313|EMBL:KGA04661.1, ECO:0000313|Proteomes:UP000029304};
RN [1] {ECO:0000313|EMBL:KGA04661.1, ECO:0000313|Proteomes:UP000029304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) 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:KGA04661.1}.
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DR EMBL; JNSD01000013; KGA04661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094PRP4; -.
DR STRING; 1504317.GM43_3895; -.
DR PATRIC; fig|1504317.4.peg.781; -.
DR Proteomes; UP000029304; 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:KGA04661.1}.
FT DOMAIN 14..312
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 462 AA; 50229 MW; 13085FE052537A58 CRC64;
MSQLGHQPLS PLDGRYRDTT APLAEFFSEA ALNRARVGVE IEWLIRLCAE GVAGTTPLPP
ATIARLRDVV THFSSADVEA IAAYEAKTKH DVKAVEYFVR DVLSAEGLES LHELVHFGCT
SEDINNVSYA LVVRDGIASV WLPALVRVHE SLRTRAVLWK AQPMLARTHG QPATPTTMGK
EVAVFAHRLS SIIERVSTQT YLAKFSGATG TFSAHVVAEP SVNWPVVSKK FVEDMGLTWN
PLTTQIESHD ALAQVLGAIS HGNKILHNLA TDMWAYISLG YVRQVPEPGT TGSSTMPHKI
NPIRFENAEA NCEISSALLD SLATTLVTSR LQRDLTDSTT QRNIGVAIGY SLLALTNIQK
GLEEIDLNTE IIAADLATHW EVLAEAVQMV IRAEIVRGSS SLKDPYAVVK ELTRGQNISE
ADLRSFIAGL DVSDPAKASL AELTPELYTG LASALVEYLE DV
//
