ID   ASPA_SERMA              Reviewed;         478 AA.
AC   P33109;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   13-SEP-2023, entry version 76.
DE   RecName: Full=Aspartate ammonia-lyase;
DE            Short=Aspartase;
DE            EC=4.3.1.1;
GN   Name=aspA;
OS   Serratia marcescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sr41;
RX   PubMed=7846149; DOI=10.1006/plas.1994.1061;
RA   Omori K., Akatsuka H., Komatsubara S.;
RT   "Construction of a versatile promoter analysis vector and its use for
RT   analysis of the Serratia marcescens aspartase promoter region.";
RL   Plasmid 32:233-237(1994).
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; D13252; BAA02518.1; -; Genomic_DNA.
DR   PIR; JS0764; JS0764.
DR   AlphaFoldDB; P33109; -.
DR   SMR; P33109; -.
DR   STRING; 273526.SMDB11_4454; -.
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.
FT   CHAIN           1..478
FT                   /note="Aspartate ammonia-lyase"
FT                   /id="PRO_0000161345"
FT   BINDING         104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         143..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  52543 MW;  254A7B455838D2A5 CRC64;
     MSNNIRIEED LLGTREVPAD AYYGVHTLRA IENFYISNSK ISDVPEFVRG MVMVKKAAAM
     ANKELKTIPR KIADVIIQAC DEVLDKGKCM DQFPVDVFQG GAGTSLNMNT NEVLANIGLE
     LMGHQKGEYQ YLNPNDHLNK CQSTNDAYPT GFRIAVYASN QKLIDAINQL REGFDRKAKE
     FETILKMGRT QLQDAVPMTL GQEFHAFSVL LNEETRNLHR TATLLLEVNL GATAIGTALN
     TPEGYQPLAV QKLAEVSGLP VVPAEDLIEA TSDCGAYVMV HSALKRLAVK LSKICNDLRL
     LSSGPRAGLN EINLPELQAG SSIMPAKVNP VVPEVVNQVC FKVIGNDTCV TMAAEAGQLQ
     LNVMEPVIGQ AMFESIHILT NACYNLLEKC INGITANKEV CEHYVFNSIG IVTYLNPFIG
     HHNGDIVGKI CAETGKSVRE VVLERGLLTE AELDDIFSVE NLMHPAYKAK RYTDENEQ
//