ID A0A099S6H4_9CLOT Unreviewed; 343 AA.
AC A0A099S6H4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KGK87483.1};
GN ORFNames=DP68_09275 {ECO:0000313|EMBL:KGK87483.1};
OS Clostridium sp. HMP27.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1487921 {ECO:0000313|EMBL:KGK87483.1, ECO:0000313|Proteomes:UP000030009};
RN [1] {ECO:0000313|EMBL:KGK87483.1, ECO:0000313|Proteomes:UP000030009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMP27 {ECO:0000313|EMBL:KGK87483.1,
RC ECO:0000313|Proteomes:UP000030009};
RA Tan B.F., Foght J., Budwill K.;
RT "Draft genome sequence of Clostridium sp. HMP27 isolated from a coal
RT degrading methanogenic culture.";
RL Submitted (APR-2014) 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}.
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:KGK87483.1}.
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DR EMBL; JMFY01000018; KGK87483.1; -; Genomic_DNA.
DR RefSeq; WP_035308768.1; NZ_JMFY01000018.1.
DR AlphaFoldDB; A0A099S6H4; -.
DR STRING; 1487921.DP68_09275; -.
DR eggNOG; COG2008; Bacteria.
DR Proteomes; UP000030009; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd06502; TA_like; 1.
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; IPR023603; Low_specificity_L-TA-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; NF041359; GntG_guanitoxin; 1.
DR PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR PIRSF; PIRSF017617; Thr_aldolase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030009}.
FT DOMAIN 5..286
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 199
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 343 AA; 38256 MW; 71A28CBDD7CF2EA9 CRC64;
MNFIDLRSDT VTKPTEEMRK AMYNAEVGDD VYEDDITVKE LEEYAAKLVN KEAALFVPTG
TFGNQLALFT HCLRGTEVIL EENCHILQHE VGAPAIIAGV QIRPLRSNKG EMNPSEVEKT
IRGEDIHFPE TSLICVENAH SNGRVISTQN MKEIYEVAKK HNLPVHLDGA RLFNASASLD
VEASDITKYC DSVMFCLSKG LCAPIGSMVA GSKEFIAKAR KKRKIMGGGM RQAGILAAAG
MVALKDMRQH LKVDHENAKF LGEELSKISG INVNLDQIHI NMVFFSIEDS SIDGKLIVDE
FYKNSIKINP PENGEFRFVT NYWVNKEHIV RCVDILKELL NAK
//
