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Database: UniProt
Entry: A0A010RS53_PSEFL
LinkDB: A0A010RS53_PSEFL
Original site: A0A010RS53_PSEFL 
ID   A0A010RS53_PSEFL        Unreviewed;       474 AA.
AC   A0A010RS53;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:EXF91779.1};
DE            EC=4.3.1.1 {ECO:0000313|EMBL:EXF91779.1};
GN   Name=aspA {ECO:0000313|EMBL:EXF91779.1};
GN   ORFNames=HK44_013300 {ECO:0000313|EMBL:EXF91779.1};
OS   Pseudomonas fluorescens HK44.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1042209 {ECO:0000313|EMBL:EXF91779.1, ECO:0000313|Proteomes:UP000022611};
RN   [1] {ECO:0000313|EMBL:EXF91779.1, ECO:0000313|Proteomes:UP000022611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HK44 {ECO:0000313|EMBL:EXF91779.1,
RC   ECO:0000313|Proteomes:UP000022611};
RX   PubMed=21742869; DOI=10.1128/JB.05530-11;
RA   Chauhan A., Layton A.C., Williams D.E., Smartt A.E., Ripp S.,
RA   Karpinets T.V., Brown S.D., Sayler G.S.;
RT   "Draft genome sequence of the polycyclic aromatic hydrocarbon-degrading,
RT   genetically engineered bioluminescent bioreporter Pseudomonas fluorescens
RT   HK44.";
RL   J. Bacteriol. 193:5009-5010(2011).
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:EXF91779.1}.
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DR   EMBL; AFOY02000019; EXF91779.1; -; Genomic_DNA.
DR   RefSeq; WP_019694323.1; NZ_AFOY02000019.1.
DR   AlphaFoldDB; A0A010RS53; -.
DR   PATRIC; fig|1042209.11.peg.5076; -.
DR   eggNOG; COG1027; Bacteria.
DR   HOGENOM; CLU_021594_4_1_6; -.
DR   OrthoDB; 9802809at2; -.
DR   Proteomes; UP000022611; Unassembled WGS sequence.
DR   GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
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; PR00145; ARGSUCLYASE.
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:EXF91779.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000022611}.
FT   DOMAIN          17..347
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          413..465
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   474 AA;  51082 MW;  0E0112CEA9B0D312 CRC64;
     MSSAASFRTE KDLLGVLEVP AQAYYGIQTL RAVNNFRLSG VPISHYPKLV VGLAMVKQAA
     ADANRELGHL SDAKHAAISE ACARLIRGDF HEEFVVDMIQ GGAGTSTNMN ANEVIANIAL
     EAMGHSKGEY QYLHPNNDVN MAQSTNDAYP TAIRLGLLLG HDALLASLDS LIQSFAAKGE
     EFSHVLKMGR TQLQDAVPMT LGQEFRAFAT TLSEDLARLK TLAPELLTEV NLGGTAIGTG
     INADPRYQHL AVERLALISG QPLVPAADLI EATSDMGAFV LFSGMLKRTA VKLSKICNDL
     RLLSSGPRTG INEINLPARQ PGSSIMPGKV NPVIPEAVNQ VAFQIIGNDL ALTIAAEGGQ
     LQLNVMEPLI AFKIFDSIRL LQRAMDMLRE HCIVGITANE ARCRELVEHS IGLVTALNPY
     IGYENATRIA RIALESGRGV LELVREEGLL DDAMLADILR PENMIAPRLV PLKA
//
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