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
//