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Database: UniProt
Entry: A0A031LXE9_9GAMM
LinkDB: A0A031LXE9_9GAMM
Original site: A0A031LXE9_9GAMM 
ID   A0A031LXE9_9GAMM        Unreviewed;       485 AA.
AC   A0A031LXE9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:EZQ12481.1};
DE            EC=4.3.1.1 {ECO:0000313|EMBL:EZQ12481.1};
GN   Name=aspA {ECO:0000313|EMBL:EZQ12481.1};
GN   ORFNames=CL42_00510 {ECO:0000313|EMBL:EZQ12481.1};
OS   Acinetobacter sp. Ver3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ12481.1, ECO:0000313|Proteomes:UP000023816};
RN   [1] {ECO:0000313|EMBL:EZQ12481.1, ECO:0000313|Proteomes:UP000023816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ver3 {ECO:0000313|EMBL:EZQ12481.1,
RC   ECO:0000313|Proteomes:UP000023816};
RA   Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT   "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT   isolated from a high altitude andean lake.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:EZQ12481.1}.
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DR   EMBL; JFYL01000001; EZQ12481.1; -; Genomic_DNA.
DR   RefSeq; WP_035263747.1; NZ_JFYL01000001.1.
DR   AlphaFoldDB; A0A031LXE9; -.
DR   eggNOG; COG1027; Bacteria.
DR   Proteomes; UP000023816; Unassembled WGS sequence.
DR   GO; GO:0008797; F:aspartate ammonia-lyase activity; IEA:UniProtKB-EC.
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; 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   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   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:EZQ12481.1}.
FT   DOMAIN          17..350
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          416..468
FT                   /note="Fumarase C C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF10415"
SQ   SEQUENCE   485 AA;  53553 MW;  94EEB22E2CE254ED CRC64;
     MSTVQFDKTR IEHDLLGEKA VPFDRYYGIH TLRAMENFQI SHQQIGENIH FIRALAQVKK
     ASAQTNLKFS KLSQDVSQAI QWACDQLIEQ PESWKSSFPI DIYQGGAGTS INMNSNEVVA
     NLALEHLGLP KGQYDVIHPN DHVNKSQSTN DVYPTALRLA TYYSLEDLLS QVRSLIAAIE
     IKASEFQHVI KMGRTQLQDA VPMTLGQEFR AFATLLKEDY RLIQKMRHLL LEINLGATAI
     GTGVNTPHGY ALEVVQTLSQ ITGLKLQGAE DYVEATSDCG VFIILSSTLK RLAVKLSKIC
     NDLRLLSSGP RTGLAEIRLP ELQAGSSIMP AKINPVIPEV VNQIAFKVIG NDLTVTMAAE
     AGQLQLNVME PVIALTINES TNLLIQAMQT LENKCIQGIT ANEQSCYDAV MRSVGIVTLL
     DPILGHAKCD EIGKVCLAEN KTIQQVVIEQ NLLTQEQLNQ IFSFENLVSE IAGHVVDDMN
     MDKVS
//
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