ID K1MGE6_9LACT Unreviewed; 471 AA.
AC K1MGE6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:EKB55109.1};
GN ORFNames=HMPREF9706_01299 {ECO:0000313|EMBL:EKB55109.1};
OS Facklamia hominis CCUG 36813.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Facklamia.
OX NCBI_TaxID=883111 {ECO:0000313|EMBL:EKB55109.1, ECO:0000313|Proteomes:UP000004465};
RN [1] {ECO:0000313|EMBL:EKB55109.1, ECO:0000313|Proteomes:UP000004465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 36813 {ECO:0000313|EMBL:EKB55109.1,
RC ECO:0000313|Proteomes:UP000004465};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Facklamia hominis CCUG 36813.";
RL Submitted (JUL-2012) 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:EKB55109.1}.
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DR EMBL; AGZD01000007; EKB55109.1; -; Genomic_DNA.
DR RefSeq; WP_006908607.1; NZ_JH932292.1.
DR AlphaFoldDB; K1MGE6; -.
DR STRING; 883111.HMPREF9706_01299; -.
DR PATRIC; fig|883111.3.peg.1307; -.
DR HOGENOM; CLU_021594_4_1_9; -.
DR OrthoDB; 9769623at2; -.
DR Proteomes; UP000004465; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; 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; 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:EKB55109.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004465}.
FT DOMAIN 18..346
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 413..464
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 471 AA; 51479 MW; 000E486210A3488A CRC64;
MTTHTNNPTR MEADSIGQHA VPVDAYYGVQ SLRARENFPI TGQSLHPRFI QSLAYVKKAC
AITNQACHRL SEDVAQAIVQ ACDEIINHQL QDAFIVDPIQ GGAGTSMNMN INEVLANRAI
EILGGQKGNY HLVHPNDHVN YGQSTNDVIP TAGKLTTYQL AQDLIQMLIQ LEEALLDKAQ
AFDDIIKMGR TQMQDAIPIR LGQEFHAYAT AIKRSRQRLE NALDELLTVN LGATAIGTGL
NADEHYFTQV VPELAEVSGL PVHQAEDMID GTQHIDSFAY ISSILKTLAL ALSKMSNDLR
LMSSGPKTGF NEINLPKKQN GSSIMPGKVN PVIPEVVNQV AFKVCGNDLT IAMAVEAGQL
ELNAFEPVTF FCLFESLTYL KQAIQTLIDN CLKDLTANRD RCHELVDQSV GTITALVPYI
GYQAAADIAK EALTSDQSVK ELVIEKGLLD QASLDHLLQA EKMTTPGICQ A
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