ID W7DYD2_9PROT Unreviewed; 475 AA.
AC W7DYD2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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:EUK17674.1};
GN ORFNames=COMX_09451 {ECO:0000313|EMBL:EUK17674.1};
OS Commensalibacter papalotli (ex Servin-Garciduenas et al. 2014).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1208583 {ECO:0000313|EMBL:EUK17674.1, ECO:0000313|Proteomes:UP000019250};
RN [1] {ECO:0000313|EMBL:EUK17674.1, ECO:0000313|Proteomes:UP000019250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX-MONARCH01 {ECO:0000313|Proteomes:UP000019250};
RX PubMed=24604647;
RA Servin-Garciduenas L.E., Sanchez-Quinto A., Martinez-Romero E.;
RT "Draft Genome Sequence of Commensalibacter papalotli MX01, a Symbiont
RT Identified from the Guts of Overwintering Monarch Butterflies.";
RL Genome Announc. 2:e00128-14(2014).
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:EUK17674.1}.
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DR EMBL; ATSX01000003; EUK17674.1; -; Genomic_DNA.
DR RefSeq; WP_034340553.1; NZ_ATSX01000003.1.
DR AlphaFoldDB; W7DYD2; -.
DR STRING; 1208583.COMX_09451; -.
DR PATRIC; fig|1208583.4.peg.1907; -.
DR eggNOG; COG1027; Bacteria.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000019250; 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:EUK17674.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019250}.
FT DOMAIN 14..346
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 412..464
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 475 AA; 51892 MW; 48A4875BE6F35A64 CRC64;
MSDQTFRTEK DLLGSMDVPS DAYYGVQTLR AINNFKLTGV PLSHFAHLVN GLAMVKWSAA
AANHKLGYLS DEKYHAIEKA CQRIIKGEFH DQFQVDMIQG GAGTSTNMNA NEVIANIALE
EMGHKKGEYQ YLHPNNDVNM AQSTNDAYPT AIRVGLLLGY DSILVSLSKL RDSFAKKGKE
FSHVIKMGRT QLQDAVPMTL GQEFNAFATT MTEDLERIRV LVPDLLCEVN LGGTAIGTGI
NADPHYQALA VEHLARITGH KLLPATDLIE ATSDMGAFVL LSGMLKRTAV KLSKICNDLR
LLSSGPRTGI NEINLPARQP GSSIMPGKVN PVIPEAVNQV AFTVIGNDLA LTLAAEGGQL
QLNVMEPLIA YKTMSSSILL IRAMDMLREL CIDGITANVE HCKNLVEHSI GLVTALNPYI
GYENATRIAR KALETGKGVL ELVREEKLLS EEELEKILKP ENMIAPHLAL SDLKH
//
