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Database: UniProt
Entry: A0A1I2V1R6_9GAMM
LinkDB: A0A1I2V1R6_9GAMM
Original site: A0A1I2V1R6_9GAMM 
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}.
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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
//
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