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Database: UniProt
Entry: A0A109JH88_9BRAD
LinkDB: A0A109JH88_9BRAD
Original site: A0A109JH88_9BRAD 
ID   A0A109JH88_9BRAD        Unreviewed;       453 AA.
AC   A0A109JH88;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=3-carboxy-cis,cis-muconate cycloisomerase {ECO:0000313|EMBL:KWV48864.1};
DE            EC=5.5.1.2 {ECO:0000313|EMBL:KWV48864.1};
GN   ORFNames=AS156_17890 {ECO:0000313|EMBL:KWV48864.1};
OS   Bradyrhizobium macuxiense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1755647 {ECO:0000313|EMBL:KWV48864.1, ECO:0000313|Proteomes:UP000057737};
RN   [1] {ECO:0000313|EMBL:KWV48864.1, ECO:0000313|Proteomes:UP000057737}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR 10303 {ECO:0000313|EMBL:KWV48864.1,
RC   ECO:0000313|Proteomes:UP000057737};
RA   Zelli J.E., Simoes-Araujo J.L., Barauna A.C., Silva K.;
RT   "Draft Genome Sequence of the Strain BR 10303 (Bradyrhizobium sp.) isolated
RT   from nodules of Centrolobium paraense.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       {ECO:0000256|ARBA:ARBA00034772}.
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:KWV48864.1}.
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DR   EMBL; LNCU01000106; KWV48864.1; -; Genomic_DNA.
DR   RefSeq; WP_066513266.1; NZ_LNCU01000106.1.
DR   AlphaFoldDB; A0A109JH88; -.
DR   OrthoDB; 9768878at2; -.
DR   Proteomes; UP000057737; Unassembled WGS sequence.
DR   GO; GO:0047472; F:3-carboxy-cis,cis-muconate cycloisomerase activity; IEA:UniProtKB-EC.
DR   CDD; cd01597; pCLME; 1.
DR   Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR   Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR   InterPro; IPR019468; AdenyloSucc_lyase_C.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR43172; ADENYLOSUCCINATE LYASE; 1.
DR   PANTHER; PTHR43172:SF2; ADENYLOSUCCINATE LYASE C-TERMINAL DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF10397; ADSL_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00145; ARGSUCLYASE.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SMART; SM00998; ADSL_C; 1.
DR   SUPFAM; SSF48557; L-aspartase-like; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:KWV48864.1}.
FT   DOMAIN          369..448
FT                   /note="Adenylosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00998"
SQ   SEQUENCE   453 AA;  49139 MW;  09D3A2F42A2605CC CRC64;
     MPAFPTSTTV LDSLLFRDAF GTSAMREVFS DLRLLQRYAE VEVALAKAEA RCGVIPADAA
     VEIAKRTDVA ALDFDRLRQE TDIVGYPILP LVHQMVKQCG EAGRYVHWGA TTQDIMDTAV
     VLQLRDGLKI VEDDIAALRS ILADLSKRYR DTPMAGRTHL QQALPVTFGY KTAIWLAAFD
     RHAERLAELK PRVLVGQFAG AAGTLASLGD KGFDVQQALC EELGLGVPVS TWHVARDGLA
     EAVNFLALVT GSLGKIALDT MIMASTEFAE VYEPFVKGRG ASSTMPQKRN PISSELMLAA
     AKAVRQHAGL MLDAMVQDFE RATGPWHAEW MAIPESFVLT AGALHQAKFA LGGLIVDEKR
     MADNLDISRG LIVAEAVMMG LAPAIGRQEA HDVVYDACRV ANDKGLMLAD ALAADPRVAS
     RIDRATIDRL TAPKNYLGLA PEMVDRVLTS TKR
//
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