ID   W9V923_9GAMM            Unreviewed;       461 AA.
AC   W9V923;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:EXJ15929.1};
GN   ORFNames=D779_0793 {ECO:0000313|EMBL:EXJ15929.1};
OS   Imhoffiella purpurea.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Imhoffiella.
OX   NCBI_TaxID=1249627 {ECO:0000313|EMBL:EXJ15929.1, ECO:0000313|Proteomes:UP000019460};
RN   [1] {ECO:0000313|EMBL:EXJ15929.1, ECO:0000313|Proteomes:UP000019460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AK35 {ECO:0000313|EMBL:EXJ15929.1,
RC   ECO:0000313|Proteomes:UP000019460};
RA   Nupur N., Khatri I., Subramanian S., Pinnaka A.;
RT   "Genome assembly of Thiorhodococcus sp. AK35.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:EXJ15929.1}.
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DR   EMBL; AONC01000018; EXJ15929.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9V923; -.
DR   STRING; 1249627.D779_0793; -.
DR   PATRIC; fig|1249627.3.peg.1367; -.
DR   eggNOG; COG1027; Bacteria.
DR   Proteomes; UP000019460; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd01357; Aspartase; 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   Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR018951; Fumarase_C_C.
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   PANTHER; PTHR42696; ASPARTATE AMMONIA-LYASE; 1.
DR   PANTHER; PTHR42696:SF2; ASPARTATE AMMONIA-LYASE; 1.
DR   Pfam; PF10415; FumaraseC_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:0000313|EMBL:EXJ15929.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019460}.
FT   DOMAIN          9..338
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          405..456
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   461 AA;  49504 MW;  9149DDF5534949C5 CRC64;
     MRIESDALGE FPVPADAYYG IHTARALANF DLLGRPCRAE LIRAMAQVKL ACARTNAELG
     FLSEAEAGAI QAACREILAG GLHPWIRVDA LQGGAGTSLN MNLNEVIANR AEERLGGSLG
     SYARVHPLHQ VNLHQSTNDV FPTALKVASL VALDRLEKGI ARLQSAFQAR EHVFEGIPKM
     GRTQLQDACP MTVGAAFGAW SEAFARDRWR VFKCKERLRV VNLGGTAIGT GLTAPRDYIF
     RVTDRLREET RLNLARAENL LDATQNADVF VEVSGILKAH AVNLYKISSD LRLLASGPRA
     GIAELRLPPV QAGSSVMPGK VNPVVCEAAA QAAMTAIGND TMITQACQSG QLELNAFLPL
     VANALLESLA VLERASLTLA ERCVDGIEVD ADHCREQVER SWAVVTALVP ALGYETASRV
     AKEAAASDRR VRDLVLEAGL LDAATLDRLL SPAAMTALGF R
//