ID A0A1Q5U0H6_9GAMM Unreviewed; 474 AA.
AC A0A1Q5U0H6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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:OKP05985.1};
GN ORFNames=Xentx_02313 {ECO:0000313|EMBL:OKP05985.1};
OS Xenorhabdus thuongxuanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1873484 {ECO:0000313|EMBL:OKP05985.1, ECO:0000313|Proteomes:UP000186277};
RN [1] {ECO:0000313|EMBL:OKP05985.1, ECO:0000313|Proteomes:UP000186277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30TX1 {ECO:0000313|EMBL:OKP05985.1,
RC ECO:0000313|Proteomes:UP000186277};
RA Kaempfer P., Tobias N.J., Phan Ke L., Bode H.B., Glaeser S.P.;
RT "Xenorhabdus thuongxuanensis sp. nov. and Xenorhabdus eapokensis sp. nov.,
RT isolated from Steinernema species.";
RL Submitted (SEP-2016) 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:OKP05985.1}.
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DR EMBL; MKGR01000016; OKP05985.1; -; Genomic_DNA.
DR RefSeq; WP_074020368.1; NZ_MKGR01000016.1.
DR AlphaFoldDB; A0A1Q5U0H6; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000186277; 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:OKP05985.1}.
FT DOMAIN 13..345
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 411..462
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 474 AA; 52022 MW; 00932644D3CAD211 CRC64;
MSNNIRIEED LLGKREVPAE AYYGIHTLRA IENFYISDRT INNVPEFIRG MVMVKKAAAL
ANKELHTIPG KVADIIVKAC DEVLIKSKCM DQFPVDVFQG GAGTSLNMNT NEVLANIGLE
LMGHQKGEYE YLNPNDHLNR SQSTNDAYPT GFRIAVYNSL MHLIDSIELL KEGFDKKGVE
FDDILKMGRT QLQDAVPMTL GQEFRAFSVL LKEEIKNINR TAELLLEVNL GATAIGTGLN
TAPGYQKLVV EKLAEVTGLP CQPAEDLIEA TSDCGAYVMV HSALKRLAVK MSKICNDLRL
LSSGPRAGLN EINLPELQAG SSIMPAKVNP VVPEVVNQVC FKVIGNDTCV TMAAEAGQLQ
LNVMEPAIGQ AMFESISILS NACRNLVEKC INGITANKEV CESFVFNSIG IVTYLNPFIG
HHNGDIVGKI CAETGKSVRE VVLERGLLTE TELDDIFSVE NLKHPTYKAK RFDD
//
