ID ASPA_PSEAE Reviewed; 474 AA.
AC Q9HTD7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Aspartate ammonia-lyase;
DE Short=Aspartase;
DE EC=4.3.1.1;
GN Name=aspA; OrderedLocusNames=PA5429;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC Aspartase subfamily. {ECO:0000305}.
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DR EMBL; AE004091; AAG08814.1; -; Genomic_DNA.
DR PIR; C82968; C82968.
DR RefSeq; NP_254116.1; NC_002516.2.
DR RefSeq; WP_003096822.1; NZ_QZGE01000012.1.
DR AlphaFoldDB; Q9HTD7; -.
DR SMR; Q9HTD7; -.
DR STRING; 208964.PA5429; -.
DR PaxDb; 208964-PA5429; -.
DR GeneID; 878603; -.
DR KEGG; pae:PA5429; -.
DR PATRIC; fig|208964.12.peg.5690; -.
DR PseudoCAP; PA5429; -.
DR HOGENOM; CLU_021594_4_1_6; -.
DR InParanoid; Q9HTD7; -.
DR OrthoDB; 9802809at2; -.
DR PhylomeDB; Q9HTD7; -.
DR BioCyc; PAER208964:G1FZ6-5556-MONOMER; -.
DR BRENDA; 4.3.1.1; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008797; F:aspartate ammonia-lyase activity; IBA:GO_Central.
DR GO; GO:0006531; P:aspartate metabolic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..474
FT /note="Aspartate ammonia-lyase"
FT /id="PRO_0000287771"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144..146
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 51070 MW; DE868A8CA8478429 CRC64;
MSPVASSRIE KDLLGTLEVP ADAYYGIQTL RAVNNFRLSG VPLSHYPKLV VALAMVKQAA
ADANRQLGHL PEDKHAAISE ACARLIRGDF HEQFVVDMIQ GGAGTSTNMN ANEVIANIAL
EAMGHTKGEY KYLHPNNDVN MAQSTNDAYP TAIRLGLLLG HDTLLASLDS LIQAFAAKGV
EFAGVLKMGR TQLQDAVPMT LGQEFHAFAT TLGEDLDRLR RLAPELLTEV NLGGTAIGTG
INADPGYQKL AVERLAAISG QPLKPAADLI EATSDMGAFV LFSGMLKRTA VKLSKICNDL
RLLSSGPRTG INEINLPPRQ PGSSIMPGKV NPVIPEAVNQ VAFEVIGNDL ALTLAAEGGQ
LQLNVMEPLI AYKIFDSIRL LQRAMDMLRE HCITGITANV ERCHELVEHS IGLVTALNPY
IGYENSTRIA KTALESGRGV LELVREEKLL DEATLADILL PENMIAPRLI PLRA
//
