ID K6U873_9CLOT Unreviewed; 465 AA.
AC K6U873;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:EKQ57927.1};
GN ORFNames=A370_00355 {ECO:0000313|EMBL:EKQ57927.1};
OS Clostridium sp. Maddingley MBC34-26.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ57927.1, ECO:0000313|Proteomes:UP000001325};
RN [1] {ECO:0000313|EMBL:EKQ57927.1, ECO:0000313|Proteomes:UP000001325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX PubMed=23405323;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA Midgley D.J., Hendry P.;
RT "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from Coal-
RT Seam Gas Formation Water.";
RL Genome Announc. 1:E00081-12(2013).
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:EKQ57927.1}.
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DR EMBL; ALXI01000008; EKQ57927.1; -; Genomic_DNA.
DR AlphaFoldDB; K6U873; -.
DR STRING; 1196322.A370_00355; -.
DR PATRIC; fig|1196322.3.peg.347; -.
DR eggNOG; COG1027; Bacteria.
DR Proteomes; UP000001325; 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, ECO:0000313|EMBL:EKQ57927.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001325}.
FT DOMAIN 13..339
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 407..458
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 465 AA; 50762 MW; D755D8B264DAF9BE CRC64;
MNYRLEQDLL GEKNIDNSTY GGINTARALE NFNLGGKTVN LNLVKEIALI KKAAAMTNKK
LKLLPPEKAD AIIKASEEII EGKFDDEFKV SAFQGGAGTS TNMNVNEVIA NRAIELLAGT
KGDYDLVHPL NHVNMSQSTN DVYPSALRIA AIKLIRKLSN SLSSLQEALQ IKENEFSDII
KLGRTQLMDA LPMTAGQGFG AYAKAIERDR WRIYKVEERL RQINLGGTAI GTGLNATNKY
VFMMTDTIQT LTGLGIARSD YPMDITQNCD IFVETSGLLK SCSVNLLKIS NDLRLLNSGP
RGGIGEVMLP NMQAGSTIMP GKVNPVIPEM VAQVSLRVIS NDSAITMASS MGQLELNAFT
PLIAECLLES LELLDKSVII FKEKCIDGLQ MDKDRCLENI ENSLVSATSL VHHVGYDKAS
LISKKALATG KTIREILLEE QILPADVIDK ILSPAELIRT HIPGK
//
