ID A0A427DYX1_9PSED Unreviewed; 474 AA.
AC A0A427DYX1;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 12.
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:RRV09001.1};
GN ORFNames=EGJ27_04280 {ECO:0000313|EMBL:RRV09001.1};
OS Pseudomonas sp. v388.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2479849 {ECO:0000313|EMBL:RRV09001.1, ECO:0000313|Proteomes:UP000268166};
RN [1] {ECO:0000313|EMBL:RRV09001.1, ECO:0000313|Proteomes:UP000268166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=v388 {ECO:0000313|Proteomes:UP000268166};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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:RRV09001.1}.
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DR EMBL; RHQN01000002; RRV09001.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427DYX1; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000268166; 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; 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:RRV09001.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000268166}.
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; 51197 MW; D3FAB2948FAC51F6 CRC64;
MSSSASSRIE KDLLGVLEVP AHAYYGIQTL RAVNNFHLSG VPLSHYPKLV VALAMVKQAA
ADANHQLGHL NDAKHAAISE ACARLIRGDF HDQFVVDMIQ GGAGTSTNMN ANEVIANIAL
ETMGFEKGEY KHLHPNNDVN MAQSTNDAYP TAIRLGLLLG HDALLASLAS LIQAFAAKGE
EFNHVLKMGR TQLQDAVPMT LGQEFRAFAT TLTEDLNRLR SLAPELLTEV NLGGTAIGTG
INADPGYQHL AVERLATISG QPLVPAADLI EATSDMGAFV LFSGMLKRTA VKLSKICNDL
RLLSSGPRTG INEINLPARQ PGSSIMPGKV NPVIPEAVNQ VAFEIIGNDL ALTMAAEGGQ
LQLNVMEPLI AYKIFDSIRL LQRAMDMLRE HCIVGITANE QRCRELVEHS IGLVTALNPY
IGYENSTRIA RIALETGRGV LELVREEGLL DDTMLDDILR PENMIAPRLA PLKA
//
