ID A0A086ZL89_9BIFI Unreviewed; 481 AA.
AC A0A086ZL89;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:KFI47289.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:KFI47289.1};
GN ORFNames=BBIA_2217 {ECO:0000313|EMBL:KFI47289.1};
OS Bifidobacterium biavatii DSM 23969.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437608 {ECO:0000313|EMBL:KFI47289.1, ECO:0000313|Proteomes:UP000029108};
RN [1] {ECO:0000313|EMBL:KFI47289.1, ECO:0000313|Proteomes:UP000029108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23969 {ECO:0000313|EMBL:KFI47289.1,
RC ECO:0000313|Proteomes:UP000029108};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
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:KFI47289.1}.
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DR EMBL; JGYN01000036; KFI47289.1; -; Genomic_DNA.
DR RefSeq; WP_051924034.1; NZ_JGYN01000036.1.
DR AlphaFoldDB; A0A086ZL89; -.
DR STRING; 1437608.GCA_000771645_00086; -.
DR eggNOG; COG1027; Bacteria.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000029108; 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; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KFI47289.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029108}.
FT DOMAIN 21..352
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 419..469
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 481 AA; 51906 MW; 40236D2C032D3FAC CRC64;
MTTQATDRNP QPTRLEHDCI GELAVPANVY WGIHTQRAIG NFTVSNIPDS AHPQLIRAYA
TVKRACAEAN AELGLIDEDK ARAIVAACLE IEGGKLADQF PVDVLQGGAG TSTNMNMNEV
IANRALEIIG RQRGDYAVIH PNDTVNHSQS TNDTYPAACK LALIDALNPL AEETRKLARA
FHDLADRHIN DVTIGRTQLQ DAVPMTYGQE FHAFASFLKT DLAELERVVP RLMSLNLGAT
AIGTGICADL RFRKTATEHL ARITGLPITA APDPVAAMTD MSAYIAVSQT VKNLAIHLKK
AADDLRLLNS GPHDGFNDLN VPARQAGSSI MPGKVNPVIP ECVDQCCFMV FGMDTTVTWA
ASEGQLQLNA FDPVMIHALL GGIDLLTRAM AMFRERCVDG ITINAEVGRR YAAYSPSIAA
TLNDAIGYEH AADIAKEAAV SGRSVREVAG ERTDLPADEL DALLDPIALS RRLGQTCREH
Q
//
