ID   ASPA_CORGL              Reviewed;         526 AA.
AC   Q59200;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Aspartate ammonia-lyase;
DE            Short=Aspartase;
DE            EC=4.3.1.1;
GN   Name=aspA; OrderedLocusNames=Cgl1503, cg1697;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MJ233;
RX   PubMed=7789816; DOI=10.1016/0378-1119(95)00117-o;
RA   Asai Y., Inui M., Vertes A., Kobayashi M., Yukawa H.;
RT   "Cloning and sequence determination of the aspartase-encoding gene from
RT   Brevibacterium flavum MJ233.";
RL   Gene 158:87-90(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Aspartase subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D25316; BAA04987.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98896.1; -; Genomic_DNA.
DR   EMBL; BX927152; CAF21511.1; -; Genomic_DNA.
DR   PIR; JC4101; JC4101.
DR   RefSeq; NP_600719.1; NC_003450.3.
DR   RefSeq; WP_011014409.1; NC_006958.1.
DR   AlphaFoldDB; Q59200; -.
DR   SMR; Q59200; -.
DR   STRING; 196627.cg1697; -.
DR   PRIDE; Q59200; -.
DR   KEGG; cgb:cg1697; -.
DR   KEGG; cgl:Cgl1503; -.
DR   PATRIC; fig|196627.13.peg.1470; -.
DR   eggNOG; COG1027; Bacteria.
DR   HOGENOM; CLU_021594_4_0_11; -.
DR   OMA; EICENYV; -.
DR   Proteomes; UP000000582; Chromosome.
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   Gene3D; 1.10.275.10; -; 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   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00839; aspA; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..526
FT                   /note="Aspartate ammonia-lyase"
FT                   /id="PRO_0000161337"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        138
FT                   /note="E -> G (in Ref. 1; BAA04987)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   526 AA;  57569 MW;  6C792698A8EA9093 CRC64;
     MSKTSNKSSA DSKNDAKAED IVNGENQIAT NESQSSDSAA VSERVVEPKT TVQKKFRIES
     DLLGELQIPS HAYYGVHTLR AVDNFQISRT TINHVPDFIR GMVQVKKAAA LANRRLHTLP
     AQKAEAIVWA CDQILIEERC MDQFPIDVFQ GGAGTSLNMN TNEVVANLAL EFLGHEKGEY
     HILHPMDDVN MSQSTNDSYP TGFRLGIYAG LQTLIAEIDE LQVAFRHKGN EFVDIIKMGR
     TQLQDAVPMS LGEEFRAFAH NLAEEQTVLR EAANRLLEVN LGATAIGTGV NTPAGYRHQV
     VAALSEVTGL ELKSARDLIE ATSDTGAYVH AHSAIKRAAM KLSKICNDLR LLSSGPRAGL
     NEINLPPRQA GSSIMPAKVN PVIPEVVNQV CFKVFGNDLT VTMAAEAGQL QLNVMEPVIG
     ESLFQSLRIL GNAAKTLREK CVVGITANAD VCRAYVDNSI GIITYLNPFL GHDIGDQIGK
     EAAETGRPVR ELILEKKLMD EKTLEAVLSK ENLMHPMFRG RLYLEN