ID A0A494YTI9_9BACI Unreviewed; 485 AA.
AC A0A494YTI9;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 13-SEP-2023, entry version 11.
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:RKQ13418.1};
GN ORFNames=D8M05_16290 {ECO:0000313|EMBL:RKQ13418.1};
OS Oceanobacillus bengalensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=1435466 {ECO:0000313|EMBL:RKQ13418.1, ECO:0000313|Proteomes:UP000281813};
RN [1] {ECO:0000313|EMBL:RKQ13418.1, ECO:0000313|Proteomes:UP000281813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1K00260 {ECO:0000313|EMBL:RKQ13418.1,
RC ECO:0000313|Proteomes:UP000281813};
RX PubMed=26303283; DOI=10.1007/s10482-015-0573-5;
RA Yongchang O., Xiang W., Wang G.;
RT "Oceanobacillus bengalensis sp. nov., a bacterium isolated from seawater of
RT the Bay of Bengal.";
RL Antonie Van Leeuwenhoek 108:1189-1196(2015).
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:RKQ13418.1}.
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DR EMBL; RBZO01000031; RKQ13418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494YTI9; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000281813; 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU362017};
KW Reference proteome {ECO:0000313|Proteomes:UP000281813}.
FT DOMAIN 16..345
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 411..464
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 485 AA; 53529 MW; ECE9FE6883833804 CRC64;
MNNKQCHFRV EKDFLGEKEV PIDAYYGIQT MRAIENFPIT GYRIDEALIR AMAIVKKSAA
LANSAVGQLD EQIADGIVNA ANEIIEGKWH DQFIVDPIQG GAGTSINMNT NEVIANRALE
LIGDQKGNYR LISPNSHVNM AQSTNDAFPT AIHLSTLTRL DQLLVVMEDL HAAFLKKAEE
FDGIIKMGRT HLQDAVPIRL GQEFAAYARV LQRDIKRISR TRENLYEVNM GATAVGTGLN
ADPDYMEKVV NYLTQYSGQP IKAVENLVDG TQNTDCYIEV SSSLKNCMVN MSKVANDLRM
MASGPRSGFG EINLPARQPG SSIMPGKVNP VMAEVLNQSA FQVTGNDLTI TLACEAGQFE
LNVMEPVIVF NLLQSIKVMT NVFTVFREYC LSGITANNNK MNDYVNNSVG IVTAINPHVG
YETAAMIADE AIRTNRPVRE IVLEKGVLTA KELDTILQPF EMTHPGIAGK ELLDKKRKEK
ELVTI
//
