ID R5LX63_9BACT Unreviewed; 475 AA.
AC R5LX63;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative aspartate ammonia-lyase {ECO:0000313|EMBL:CCY83803.1};
GN ORFNames=BN473_00595 {ECO:0000313|EMBL:CCY83803.1};
OS Prevotella sp. CAG:1185.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1262921 {ECO:0000313|EMBL:CCY83803.1, ECO:0000313|Proteomes:UP000018054};
RN [1] {ECO:0000313|EMBL:CCY83803.1, ECO:0000313|Proteomes:UP000018054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:1185 {ECO:0000313|Proteomes:UP000018054};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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:CCY83803.1}.
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DR EMBL; CAYW010000190; CCY83803.1; -; Genomic_DNA.
DR AlphaFoldDB; R5LX63; -.
DR STRING; 1262921.BN473_00595; -.
DR Proteomes; UP000018054; 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; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:CCY83803.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018054}.
FT DOMAIN 16..346
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 412..464
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 475 AA; 51572 MW; 43C57F710E747DD6 CRC64;
MNSEKVTRME HDLLGSREIP ADALYGIQTL RGVENFSISK FNLSQYPLFI NGLAYTKWAA
AEANHQLGLL TDAQYEGIKA ACQDILAGKY HDQFPVDMIQ GGAGTSTNMN ANEVIANIAL
KHMGFKPGDY EHCSPHDHVN RSQSTNDAYP TAIHMGLYAS HLALVPHIKE LIAAFRKKSE
EFAHIVKMGR TQLEDAVPMT LGQTFSGFAS ILEAELLHLD QAAADFLEVN MGATAIGTGI
CSEPGYADKC VKALAEITGW DITLAKDLVG VTSDTSCMIG YMSELKRIAV KLSKISNDLR
LLASGPRCGL AEINLPARQP GSSIMPGKVN PVIPEVVSQV AFKIIGNELC VTMAGEAAQM
ELNAMEPVMA QCSFESVDLM ANACDTLRTL CVEGITSNED NCRREVNRSI GIVTALNPYI
GYEHSTEIAK KAMETGRGVV ELVLEEGILT QKDLDTILDA KNMVRPVKLD IHPKC
//
