ID A0A0Q6PPN0_9MICO Unreviewed; 460 AA.
AC A0A0Q6PPN0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:KQV06740.1};
GN ORFNames=ASC63_04930 {ECO:0000313|EMBL:KQV06740.1};
OS Leifsonia sp. Root112D2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736426 {ECO:0000313|EMBL:KQV06740.1, ECO:0000313|Proteomes:UP000051914};
RN [1] {ECO:0000313|EMBL:KQV06740.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV06740.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV06740.1, ECO:0000313|Proteomes:UP000051914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root112D2 {ECO:0000313|EMBL:KQV06740.1,
RC ECO:0000313|Proteomes:UP000051914};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQV06740.1}.
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DR EMBL; LMCU01000001; KQV06740.1; -; Genomic_DNA.
DR RefSeq; WP_055810458.1; NZ_LMCU01000001.1.
DR AlphaFoldDB; A0A0Q6PPN0; -.
DR STRING; 1736426.ASC63_04930; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000051914; 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:KQV06740.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051914}.
FT DOMAIN 15..308
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 329..448
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
SQ SEQUENCE 460 AA; 50055 MW; 26575619DF4A303F CRC64;
MTTLPPQPLS PLDGRYRAAV TELGDHLSEA GLNRARVHVE VEWLIYLTGH RMFGAEPLSD
AKIASLRGLV TDFGQPEIDE LATLEATTRH DVKAVEYLVR SRLHALGLDA IAELTHFAAT
SEDINNLSYA LTVKAAVTAV WLPKLDAVLA VLREMAEKHR ADAMLARTHG QPATPTTMGK
ELAVFVYRLQ RIRSQIEGTE YLGKFSGATG TFAAHLAADP SADWPAISRE FVESLGLDWN
PLTTQIESHD WQAELYARVS HANRVLHNLA TDVWTYISLG YFRQIPQAGA TGSSTMPHKI
NPIRFENAEA NLELSSAVLD SLAATLVTSR LQRDLTDSTT QRNIGVGLGH SLLALDNLQR
GLGEIDLDAG LLASDLDANW EILGEAIQTV IRAEVTAGRS SIEDPYAMLK ELTRGKRIGA
GDLARFVEAL DIGEDARARL LALTPAGYAG LADALVNYLD
//
