ID A0A0Q5LAF4_9MICO Unreviewed; 460 AA.
AC A0A0Q5LAF4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Adenylosuccinate lyase {ECO:0000313|EMBL:KQR44675.1};
GN ORFNames=ASF82_14870 {ECO:0000313|EMBL:KQR44675.1};
OS Frigoribacterium sp. Leaf164.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=1736282 {ECO:0000313|EMBL:KQR44675.1, ECO:0000313|Proteomes:UP000051005};
RN [1] {ECO:0000313|EMBL:KQR44675.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR44675.1,
RC ECO:0000313|Proteomes:UP000051005};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR44675.1, ECO:0000313|Proteomes:UP000051005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf164 {ECO:0000313|EMBL:KQR44675.1,
RC ECO:0000313|Proteomes:UP000051005};
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:KQR44675.1}.
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DR EMBL; LMOX01000003; KQR44675.1; -; Genomic_DNA.
DR RefSeq; WP_056058666.1; NZ_LMOX01000003.1.
DR AlphaFoldDB; A0A0Q5LAF4; -.
DR STRING; 1736282.ASF82_14870; -.
DR OrthoDB; 9768878at2; -.
DR Proteomes; UP000051005; 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:KQR44675.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051005}.
FT DOMAIN 63..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; 49955 MW; 39FB592F8DA5F42D CRC64;
MTLPPQPLSP LDGRYRASVG LLGDHLSEAG LNRARVHVEV EWLIAQTDRR AFGSSPLDEG
QKAALRAVVT DFGQEAIDEL AGLEATTRHD VKAVEYYVRA RLADLGLEGI AELTHFACTS
EDINNLSYAL TVKQAVTEVW LPAFDAVQEA LAGWATEARD VPMLAHTHGQ PATPTTVGKE
FAVFVHRLRR LRAQIEGTEY LGKFSGATGT FSAHVVADPS ADWPEVSREF VEERLGLTWN
PLTTQIESHD WQAELYSRVA HVNRVLHNLA TDIWTYISMG YFTQIPIAGS TGSSTMPHKI
NPIRFENAEA NLELSCALLD SLAATLVTSR QQRDLTDSST QRNIGVAFGH SMLALDNLRR
GLGEIAVGTA ALEADLEGNW EVLGEAIQTV VRAEVVAGRS SIADPYAMLK ELTRGRRVGQ
AELVAFVEGL DIGADAKARL VALTPAGYTG IASQLVDRLA
//
