ID A0A087DB00_9BIFI Unreviewed; 476 AA.
AC A0A087DB00;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Aspartate ammonia-lyase {ECO:0000313|EMBL:KFI92700.1};
DE EC=4.3.1.1 {ECO:0000313|EMBL:KFI92700.1};
GN ORFNames=BISA_0392 {ECO:0000313|EMBL:KFI92700.1};
OS Bifidobacterium saguini DSM 23967.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437607 {ECO:0000313|EMBL:KFI92700.1, ECO:0000313|Proteomes:UP000029066};
RN [1] {ECO:0000313|EMBL:KFI92700.1, ECO:0000313|Proteomes:UP000029066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23967 {ECO:0000313|EMBL:KFI92700.1,
RC ECO:0000313|Proteomes:UP000029066};
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:KFI92700.1}.
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DR EMBL; JGZN01000007; KFI92700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087DB00; -.
DR STRING; 1437607.BISA_0392; -.
DR OrthoDB; 9802809at2; -.
DR Proteomes; UP000029066; 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:KFI92700.1}.
FT DOMAIN 15..346
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 414..464
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 476 AA; 51331 MW; 2B4AD900DF6AB116 CRC64;
MSEHITTRLE HDCIGTLEVP DNVYWGIHTQ RAIENFPVSG ITDGQHPELI RAYATVKRAC
AIANEELGLL DHAKAVAIRQ ACQEIELGKL ADQFPVDVMQ GGAGTSSNMN MNEVIANRAL
EIAGHKRGDY HYIHPNDDVN ESQSTNDTYP AACKLALIDA IGPLAEATKK LAKAFHDLAD
KHINDVTIGR TQLQDAVPMT YGQEFHSFAT LLKSDLAAFD RVVPLLAQLN LGATAIGTGI
CADLRFRKSA TEHLANITGL PITAAPDPVA AMTDMGAYVA TSAAVKSLAV HLKKAADDLR
LLNSGPRCGF NDLNVPARQA GSSIMPAKVN PVIPECVNQC CFSIFGMDVT VNWAVAEGQL
QLNAFDPLMV HELLTGMALL TRAMTIFRTN CVEGIEINAE IGRAYAQSSP SISAALNHYI
GYEKAADIAA EAVHTGRTVR EVAGERTDLP AEQLDEILDP IRLARGLGQT CREHQE
//
