ID A0A095ZL44_9BACT Unreviewed; 470 AA.
AC A0A095ZL44;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:KGF19302.1};
GN ORFNames=HMPREF1640_00280 {ECO:0000313|EMBL:KGF19302.1};
OS Prevotella sp. S7-1-8.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1284775 {ECO:0000313|EMBL:KGF19302.1, ECO:0000313|Proteomes:UP000029597};
RN [1] {ECO:0000313|EMBL:KGF19302.1, ECO:0000313|Proteomes:UP000029597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7-1-8 {ECO:0000313|EMBL:KGF19302.1,
RC ECO:0000313|Proteomes:UP000029597};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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:KGF19302.1}.
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DR EMBL; JRNC01000002; KGF19302.1; -; Genomic_DNA.
DR RefSeq; WP_036891394.1; NZ_JRNC01000002.1.
DR AlphaFoldDB; A0A095ZL44; -.
DR eggNOG; COG1027; Bacteria.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000029597; 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:KGF19302.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029597}.
FT DOMAIN 15..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 470 AA; 51282 MW; 83DBAB13458605D9 CRC64;
MEKNAKFRVE SDLLGELQVP AEAYYGVQTQ RAINNYKISN SKMCDYPEFV ISIAYVKKAA
AAANAELGAL DKNIAEGICK AADEVIGGKL WENFPVDMMQ GGAGTSVNMN ANEVIANRAL
ELMGYEKGDY PHCYPNDHVN CGQSTNDAYP TALRYAVYRM NKDLLKSLKQ LADAFRAKGE
EFKEDVKMGR TQLQDAVPMT SGQEFTAFAN TLQDEIAHIE YNAKLLLTIN MGATAIGTGL
NAVPGYADLV TKLLCQYTGD EFKKADDMIA ATPDTSDYVG YSGALKRLAA KLSKICNDLR
LMASGPRCGL NEINLPPMAP GSSIMPGKVN PVIPEVTNQV CFKVIGNDTT VTLAAEAGQL
QLNVMEPVIV ECLFENVSWL TNAMNTLREK CVQGITVNAK HNMDTVKHSI GIVTALNPYI
GYKNSTKVAK EALETGKSLH EIVLEKKLLT EEQVDEILDP KAMLTAHNKI
//