ID A0A1I2V1R6_9GAMM Unreviewed; 615 AA.
AC A0A1I2V1R6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Aspartate ammonia-lyase {ECO:0000256|ARBA:ARBA00016146};
DE EC=4.3.1.1 {ECO:0000256|ARBA:ARBA00012992};
GN ORFNames=SAMN05216175_11521 {ECO:0000313|EMBL:SFG83358.1};
OS Neptunomonas qingdaonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Neptunomonas.
OX NCBI_TaxID=1045558 {ECO:0000313|EMBL:SFG83358.1, ECO:0000313|Proteomes:UP000198623};
RN [1] {ECO:0000313|Proteomes:UP000198623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10971 {ECO:0000313|Proteomes:UP000198623};
RA Varghese N., Submissions S.;
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 -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC Aspartase subfamily. {ECO:0000256|ARBA:ARBA00005596}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOOU01000015; SFG83358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2V1R6; -.
DR STRING; 1045558.SAMN05216175_11521; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000198623; 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; IPR018490; cNMP-bd_dom_sf.
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; SSF51206; cAMP-binding domain-like; 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:SFG83358.1}.
FT DOMAIN 151..482
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 548..600
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 615 AA; 67468 MW; 66E57E7E1A4EF801 CRC64;
MNANNKKLIK TVLQCDSLEA PQFSGLLKLC SVREIKKGES IVTENCAERL LILLAGICQH
TESGSQVQLT GPVLCNPLIL PDNSAWLGDF MAITDATVVF VDRNRLLSWC EGSPVTVEIG
AVLLQLEKQR QEFADQRVCT KLVRREKDLL GERDVPQSAL FGVQTLRAQE NFEITGIKLM
HFPKLVNALA MVKKAAAKAN NKLGLLDDIK TRAIGQACDE IIDGQWHEHF VVDVIQGGAG
TSTNMNANEV IANRGLEILG HSRGDYQHLH PNNHVNLSQS TNDAYPTAIR LGILLSHEEY
VTALSELCYE LKQKAVEFSG VIKMGRTQLQ DAVPITLGQE FDAWYFTIKE DIEEAKDVVE
YFREINLGAT AIGTGINTDP EYSSLAIEEL CRISGKEMVR ARNLIEATSD MGAFVTFSSV
LKRNAVKLSK ICNDLRLLSS GPRAGFQEIN LPPMQPGSSI MPGKVNPVIP EMVNQVAFQI
IGNDITVTMA AEAGQLQLNV MEPVIAFNVL QSLRLQIRAV KTLASKCIKG ITANEEHCLN
TVNNSIGIIT ALNPYIGYEN ATRIAKQAIQ QNSSVRDLVL AEGLLSLADL DDILSVENMT
APRRVRKSAV NNNAV
//