ID E9RWP2_9FIRM Unreviewed; 461 AA.
AC E9RWP2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Aspartate ammonia-lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF0490_01879 {ECO:0000313|EMBL:EGC74457.1};
OS Lachnospiraceae bacterium 6_1_37FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658656 {ECO:0000313|EMBL:EGC74457.1, ECO:0000313|Proteomes:UP000006471};
RN [1] {ECO:0000313|EMBL:EGC74457.1, ECO:0000313|Proteomes:UP000006471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6_1_37FAA {ECO:0000313|EMBL:EGC74457.1,
RC ECO:0000313|Proteomes:UP000006471};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Ambrose C., Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J.,
RA Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 6_1_37FAA.";
RL Submitted (JAN-2011) 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:EGC74457.1}.
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DR EMBL; ADCR01000019; EGC74457.1; -; Genomic_DNA.
DR RefSeq; WP_008976640.1; NZ_JAQFAJ010000005.1.
DR AlphaFoldDB; E9RWP2; -.
DR STRING; 658656.HMPREF0490_01879; -.
DR GeneID; 83602897; -.
DR HOGENOM; CLU_021594_4_1_9; -.
DR Proteomes; UP000006471; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT DOMAIN 13..340
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 408..459
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 461 AA; 49870 MW; 0B7587CE68B85187 CRC64;
MKTRLEADSI GILEVPADAY YGVQSLRAKH NFPITSRPLH PEFIKSIVIL KKAAALTNEN
AGELSSEVSE AICTACDEIL EGKLFDQFIV DAIQGGAGTS ANMNANEVIA NRADELLGGT
KGSYQHVHPN DHVNMAQSTN DIIPSAGKLT VLKLLVPLFR ELERLLNALL EKSKQFDHIL
KMGRTQLQDA VPMRLGQSFH AYASVIQRDI HRLENAQKEM YRLNMGGTAI GTAINVSHSY
LQHICPKIAE LTGLPFASAD DLFDATQNLD GFVTVSSSLK TCAVNLSKLC NDLRLLSSGP
RTGFAEITLP PKQNGSSIMP GKINPVIPEV VSQVAFNIIG NDCTITMAAE AGQLELNAFE
PVVFYNLFES IETLTSAVQT LTDNCILGIT ANEKHCEELV DASVGISTAL CPTIGYKPSA
EIAKESLKTG IPVRKLVIEK GLLCPSEADV LLNPFTMTEP Q
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