ID A0A1I1ZEK8_9BACI Unreviewed; 472 AA.
AC A0A1I1ZEK8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=SAMN05192532_101194 {ECO:0000313|EMBL:SFE30022.1};
OS Alteribacillus iranensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacillus.
OX NCBI_TaxID=930128 {ECO:0000313|EMBL:SFE30022.1, ECO:0000313|Proteomes:UP000199516};
RN [1] {ECO:0000313|EMBL:SFE30022.1, ECO:0000313|Proteomes:UP000199516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23995 {ECO:0000313|EMBL:SFE30022.1,
RC ECO:0000313|Proteomes:UP000199516};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FONT01000001; SFE30022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1ZEK8; -.
DR STRING; 930128.SAMN05192532_101194; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000199516; 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362017};
KW Reference proteome {ECO:0000313|Proteomes:UP000199516}.
FT DOMAIN 12..341
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 407..460
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 472 AA; 51788 MW; 220A24D8ECD88E03 CRC64;
MAEYRTERDF LGEKQVPAEA YYGIQTIRAK ENFPITGYPP HPELIKAFGY VKKAAAMANR
DVGVLNQRIA EAVIQASDEV IEGKFNDQFI VDAIQGGAGT SFNMNANEVI ANRAIEILGD
KKGNYMVVSP NTHVNMAQST NDSFPTAIHI ASLHLAQGLT KVLDELIVSL EDKEKEFDTV
IKMGRTHLQD AVPIRLGQEF GAYKRVLKRD FSRISRSVES LHEINMGATA VGTGLNAKPE
YIEKVAQYLA DLTEMPFHSA ENLVDATQNT DAYTELSAAL KVHAINLSKM ANDLRLMSSG
PRTGLNEINL PARQPGSSIM PGKVNPVMAE VMNQISFQVI GNDHTISLAS EAGQLELNVM
EPVLVFNLLQ SLSVLQNGLN VFREHAVNGI TANVERCKEL VEKSVGIITA INPHVGYETA
SRIAKEAIET GRSVREICLE RGILSEEELD EILDAKEMTR PGIAGARFMN LE
//
