ID F7NM99_9FIRM Unreviewed; 468 AA.
AC F7NM99;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:EGO62837.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:EGO62837.1};
GN Name=aspA {ECO:0000313|EMBL:EGO62837.1};
GN ORFNames=ALO_16132 {ECO:0000313|EMBL:EGO62837.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO62837.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO62837.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO62837.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
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:EGO62837.1}.
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; AFGF01000163; EGO62837.1; -; Genomic_DNA.
DR RefSeq; WP_004097514.1; NZ_AFGF01000163.1.
DR AlphaFoldDB; F7NM99; -.
DR STRING; 1009370.ALO_16132; -.
DR eggNOG; COG1027; Bacteria.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000003240; 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:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EGO62837.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240}.
FT DOMAIN 9..338
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 404..457
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 468 AA; 50806 MW; B3C7AD376D9C70F1 CRC64;
MRFEHDLLGE IEVPDHAYYG VQTLRAMQNF KITGQRLDTD FIDSLAIVKK AAAKANMATG
RLDKAVGTVL VAAADEIISG KLHDQFCVDP IQGGAGTSVN MNMNEVLSNR ALELLGDQKG
NYTRISPNNH ANMAQSTNDA FPTAIKVCAV RKGRFLVQAL RTLAQALDEK AAEFKDVLKM
GRTHLQDAVP ITLGQEFAAY ASAVRRGAGR IEDVLQRLYA VNMGATAVGT GLNAEPAYIR
EVARQLAELT GEPFATAENL VDATNNTDAF ADMSGALKVT ALALIKMAND FRLMASGPRC
GLNELALPPR QPGSSIMPGK VNPVIPEVLN QTCYQVIGND LAVTLGVENG QFELNVMEPV
VAFNIFNSLT YLTNAVNTFN QLCVQGVQAQ REQCAQWLER SVGIVTALLP HIGYENSSRL
AEEAYKTGQP VRELILKKKL LTKEEMDMIL SPEKMTQPGI AGKKLVNM
//
