ID B7GU11_BIFLS Unreviewed; 477 AA.
AC B7GU11; E8MPA3;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Fumarate lyase {ECO:0000313|EMBL:ACJ51452.1};
GN OrderedLocusNames=Blon_0327 {ECO:0000313|EMBL:ACJ51452.1};
OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM
OS 1222 / NCTC 11817 / S12).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=391904 {ECO:0000313|EMBL:ACJ51452.1, ECO:0000313|Proteomes:UP000001360};
RN [1] {ECO:0000313|EMBL:ACJ51452.1, ECO:0000313|Proteomes:UP000001360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12 [JGI]
RC {ECO:0000313|Proteomes:UP000001360};
RX PubMed=19033196; DOI=10.1073/pnas.0809584105;
RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R.,
RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P.,
RA Richardson P.M., Mills D.A.;
RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals
RT adaptations for milk utilization within the infant microbiome.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008).
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DR EMBL; CP001095; ACJ51452.1; -; Genomic_DNA.
DR RefSeq; WP_012576760.1; NZ_JDTT01000024.1.
DR AlphaFoldDB; B7GU11; -.
DR KEGG; bln:Blon_0327; -.
DR PATRIC; fig|391904.8.peg.336; -.
DR Proteomes; UP000001360; Chromosome.
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:ACJ51452.1}.
FT DOMAIN 16..347
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 413..465
FT /note="Fumarase C C-terminal"
FT /evidence="ECO:0000259|Pfam:PF10415"
SQ SEQUENCE 477 AA; 51310 MW; 20F465EDA9748B2F CRC64;
MSETSNKTRL EHDCIGQMEV PANVYWGIHT QRAIGNFPVS GITDSQHPEL IRAYATVKRA
CAIANEELGL IDPAKAEAIR SACLEIEAGK LADQFPVDVM QGGAGTSSNM NMNEVIANRA
LEIAGHQRGD YTYIHPNDDV NESQSTNDTY PAACKLALID AIGPLAESTK KLAKAFHDLA
DKHINDVTIG RTQLQDAVPM TYGQEFHSFA TLLKSDLAAF DRVVPLLAQL NLGATAIGTG
ICADLRFRKS AIKHLAHITG LPVTAAPDPV AAMTDMGAYV ATSAAIKSLA VHLKKAADDL
RLLNSGPRCG FNDLNVPARQ AGSSIMPAKV NPVIPECVNQ CCFTIFGMDV TVNWAVAEGQ
LQLNAFDPVM VHELLTGMAL LTRAMETFRV NCVEGIEIHV GLGRSYAQSS PSIAAALNHY
IGYEHAADIA AEAVRTGRTV REVAGERTDL PAEQLDEILD PIRLARGLGQ TCREHRD
//
