ID D7N8E5_9FIRM Unreviewed; 338 AA.
AC D7N8E5;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Beta-eliminating lyase {ECO:0000313|EMBL:EFI41714.1};
GN ORFNames=HMPREF0629_00338 {ECO:0000313|EMBL:EFI41714.1};
OS Peptoniphilus sp. oral taxon 386 str. F0131.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=575609 {ECO:0000313|EMBL:EFI41714.1, ECO:0000313|Proteomes:UP000004712};
RN [1] {ECO:0000313|EMBL:EFI41714.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0131 {ECO:0000313|EMBL:EFI41714.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F.E., Haas B.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Peptoniphilus sp. oral taxon 386 strain F0131.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; GL349422; EFI41714.1; -; Genomic_DNA.
DR RefSeq; WP_009221653.1; NZ_GL349422.1.
DR AlphaFoldDB; D7N8E5; -.
DR STRING; 575609.HMPREF0629_00338; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_049619_1_0_9; -.
DR Proteomes; UP000004712; Miscellaneous, Scaffold supercont1.1.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:EFI41714.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004712}.
FT DOMAIN 25..286
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 338 AA; 38280 MW; B011A4F4CEE40F6F CRC64;
MNIFLNDYND LCHEEVYKKL ALVNQKGNAG YGNDEYCERA KQLIKRDLKN DNVHIEFVSG
GTVANIIAIS ANLLPYESVI AAASGHITGH EAGSIEATGH KIEIINTEDG KLNDILLEKK
IDELTEEYHT VPKIVYISQT TELGSVYSYA EIEDIYNVCL ERGLYLYIDG ARMAHGLAAS
DIEIEDLCNI CDIFTLGGTK NGAIYGEVLV IVEPELKQNI RNFMKQRGAV MAKSFAIGAQ
FDALFENGLY YKLADKAYDM SVKLVRELKN IGVKFFKEPE SNQVFIIYPL EKIKQLEIEN
RFEVMPYLEN EKIIRFVTNY RTTEDEINGL IKCIKELE
//
