ID B7HMI0_BACC7 Unreviewed; 479 AA.
AC B7HMI0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
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=aspA2 {ECO:0000313|EMBL:ACJ78679.1};
GN OrderedLocusNames=BCAH187_A1921 {ECO:0000313|EMBL:ACJ78679.1};
OS Bacillus cereus (strain AH187).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ78679.1, ECO:0000313|Proteomes:UP000002214};
RN [1] {ECO:0000313|EMBL:ACJ78679.1, ECO:0000313|Proteomes:UP000002214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187 {ECO:0000313|EMBL:ACJ78679.1,
RC ECO:0000313|Proteomes:UP000002214};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-2008) 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; CP001177; ACJ78679.1; -; Genomic_DNA.
DR AlphaFoldDB; B7HMI0; -.
DR KEGG; bcr:BCAH187_A1921; -.
DR HOGENOM; CLU_021594_4_1_9; -.
DR Proteomes; UP000002214; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362017}.
FT DOMAIN 19..348
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 414..467
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 479 AA; 52293 MW; F750EB99370E7E42 CRC64;
MATLTEVKNG VRIEKDFLGE KEVPNYAYYG VQTMRAVENF PITGYKIHEG LIKAFAIVKK
AAALANTDVG RLELNKGGAI AEAAQEILDG KWHDHFIVDP IQGGAGTSMN MNANEVIANR
ALELLGMEKG DYHYISPNSH VNMAQSTNDA FPTAIHIATL NALEGLLQTM GYMHDVFELK
AEQFDHVIKM GRTHLQDAVP IRLGQEFKAY SRVLERDMKR IQQSRQHLYE VNMGATAVGT
GLNADPEYIE AVVKHLAAIS ELPLVGAEDL VDATQNTDAY TEVSAALKVC MMNMSKIAND
LRLMASGPRV GLAEIMLPAR QPGSSIMPGK VNPVMPEVIN QIAFQVIGND HTICLASEAG
QLELNVMEPV LVFNLLQSIS IMNNGFRAFT DNCLKGIEAN EDRLKEYVEK SVGIITAVNP
HIGYEAAARV AKEAIATGQS VRELCVKNGV LSQEDLELIL DPFEMTHPGI AGATLLKKN
//
