ID A0A3S0JEU3_9PROT Unreviewed; 475 AA.
AC A0A3S0JEU3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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:RTR15848.1};
GN ORFNames=EJ903_22195 {ECO:0000313|EMBL:RTR15848.1};
OS Azospirillum griseum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2496639 {ECO:0000313|EMBL:RTR15848.1, ECO:0000313|Proteomes:UP000277007};
RN [1] {ECO:0000313|EMBL:RTR15848.1, ECO:0000313|Proteomes:UP000277007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-25-5w-1 {ECO:0000313|EMBL:RTR15848.1,
RC ECO:0000313|Proteomes:UP000277007};
RA Yang Y.;
RL Submitted (DEC-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:RTR15848.1}.
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DR EMBL; RXMA01000030; RTR15848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0JEU3; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000277007; 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:RTR15848.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000277007}.
FT DOMAIN 18..348
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 414..466
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 475 AA; 50678 MW; 22D3B1C95AB6C701 CRC64;
MPAAATRPTR LEHDLLGDRE VPADAYYGVH TLRAVENFPI TGTPIGHYPD LVRALADIKT
AAARANQELG LLSAERADAI AAACREIRGG ALLDHFVVDV IQGGAGTSTN MNANEVIANR
ALEILGHARG AYSHLHPNEH VNMSQSTNDV YPTALKLATY TGIFRLVEAM GYLRAAFQRK
ADEFADVLKM GRTQLQDAVP MTLGQEFSTY AVMLAEDEER LKEAALLIRE INLGATAIGT
GINAHPDYAP LVCRRLAEIS GVPVVTAPNL IEATQDCGSF VQLSGVLKRV AVKLSKTCND
LRLLSSGPRA GLGEINLPAR QAGSSIMPGK VNPVIPEVVN QIAFEVIGND MTVTFAAEAG
QLQLNAFEPI IAHSLFKSIT HLRQGCRVLA DLCVDGITAN RDHLAAAVRN SIGIVTALNP
YIGYANATEI AAEAHRTGKG VAELVEARGL MTAEALAEVL RPDILTRPQM IPTAG
//
