ID N9TZ62_9GAMM Unreviewed; 479 AA.
AC N9TZ62;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Aspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00016146, ECO:0000256|RuleBase:RU362017};
DE Short=Aspartase {ECO:0000256|RuleBase:RU362017};
DE EC=4.3.1.1 {ECO:0000256|ARBA:ARBA00012992, ECO:0000256|RuleBase:RU362017};
GN Name=aspA {ECO:0000313|EMBL:ENY71345.1};
GN ORFNames=G114_13718 {ECO:0000313|EMBL:ENY71345.1};
OS Aeromonas diversa CDC 2478-85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY71345.1, ECO:0000313|Proteomes:UP000023775};
RN [1] {ECO:0000313|EMBL:ENY71345.1, ECO:0000313|Proteomes:UP000023775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2478-85 {ECO:0000313|EMBL:ENY71345.1,
RC ECO:0000313|Proteomes:UP000023775};
RX PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA Fuste M.C.;
RT "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL Genome Announc. 1:S69-S82(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartate = fumarate + NH4(+); Xref=Rhea:RHEA:16601,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29806, ChEBI:CHEBI:29991; EC=4.3.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001494,
CC ECO:0000256|RuleBase:RU362017};
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC Aspartase subfamily. {ECO:0000256|ARBA:ARBA00005596,
CC ECO:0000256|RuleBase:RU362017}.
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:ENY71345.1}.
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DR EMBL; APVG01000037; ENY71345.1; -; Genomic_DNA.
DR RefSeq; WP_005356149.1; NZ_CDCE01000009.1.
DR AlphaFoldDB; N9TZ62; -.
DR PATRIC; fig|1268237.3.peg.2699; -.
DR eggNOG; COG1027; Bacteria.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000023775; Unassembled WGS sequence.
DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro.
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; IPR004708; ApsA.
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 NCBIfam; TIGR00839; aspA; 1.
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 3: Inferred from homology;
KW Lyase {ECO:0000256|RuleBase:RU362017, ECO:0000313|EMBL:ENY71345.1}.
FT DOMAIN 15..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 479 AA; 52396 MW; EFD94349EB91A4DB CRC64;
MSDNKNVRIE EDLLGTKEVS NDVYYGVHTL RAIENFKISS QKISDVPAFV RGMVLTKKAA
ALANGELGTI RPEIADKIVE ACDVMLNTGK CFDQFPIDVF QGGAGTSVNM NTNEVLANIA
LELMGLEKGR YDVINPNDHV NKCQSTNDAY PTGFRVAVVD STDTTLHALE HLIAAFDAKA
AEFKSILKMG RTQLQDAVPM TLGQEFHAFA VTLREEIKTI KRCQELLLEV NLGATAIGTG
LNTPPEYSQL AIQRLAEITG RAYVPAEDLI EATSDCGAYV MLHGAVKRLA MKLSKICNDL
RLLSSGPRTA LKEINLPEMQ AGSSIMPAKV NPVIPEVVNQ SCFKVFGNDV TITFAAEAGQ
LQLNVMEPVI AQAMFESLSL MEKACISLRE KCVEGITANP EICRNHVLNS IGIVTYLNPF
IGHHEGDIVG KICAQTGKNV REVVLERGLL TAEQLDEILS IENLMNPQYK AKRFTREQA
//
