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Database: UniProt
Entry: F4UXX5_ECOLX
LinkDB: F4UXX5_ECOLX
Original site: F4UXX5_ECOLX 
ID   F4UXX5_ECOLX            Unreviewed;       493 AA.
AC   F4UXX5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ORFNames=ECNG_01217 {ECO:0000313|EMBL:EGI42494.1};
OS   Escherichia coli TA280.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=656444 {ECO:0000313|EMBL:EGI42494.1, ECO:0000313|Proteomes:UP000004877};
RN   [1] {ECO:0000313|EMBL:EGI42494.1, ECO:0000313|Proteomes:UP000004877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TA280 {ECO:0000313|EMBL:EGI42494.1,
RC   ECO:0000313|Proteomes:UP000004877};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Escherichia coli TA280.";
RL   Submitted (JAN-2010) 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}.
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DR   EMBL; GL884332; EGI42494.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4UXX5; -.
DR   HOGENOM; CLU_021594_4_0_6; -.
DR   Proteomes; UP000004877; 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:EGI42494.1}.
FT   DOMAIN          28..360
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          426..479
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   493 AA;  54064 MW;  3CE9856B4304646C CRC64;
     MCLKQIIGSL KKKVHMSNNI RIEEDLLGTR EVPADAYYGV HTLRAIENFY ISNNKISDIP
     EFVRGMVMVK KAAAMANKEL QTIPKSVANA IIAACDEVLN NGKCMDQFPV DVYQGGAGTS
     VNMNTNEVLA NIGLELMGHQ KGEYQYLNPN DHVNKCQSTN DAYPTGFRIA VYSSLIKLVD
     AINQLREGFE RKAVEFQDIL KMGRTQLQDA VPMTLGQEFR AFSILLKEEV KNIQRTAELL
     LEVNLGATAI GTGLNTPKEY SPLAVKKLAE VTGFPCVPAE DLIEATSDCG AYVMVHGALK
     RLAVKMSKIC NDLRLLSSGP RAGLNEINLP ELQAGSSIMP AKVNPVVPEV VNQVCFKVIG
     NDTTVTMAAE AGQLQLNVME PVIGQAMFES VHILTNACYN LLEKCINGIT ANKEVCEGYV
     YNSIGIVTYL NPFIGHHNGD IVGKICAETG KSVREVVLER GLLTEAELDD IFSVQNLMHP
     AYKAKRYTDE SEQ
//
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