ID F2NRB3_MARHT Unreviewed; 341 AA.
AC F2NRB3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Threonine aldolase {ECO:0000313|EMBL:AEB12962.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:AEB12962.1};
GN OrderedLocusNames=Marky_2242 {ECO:0000313|EMBL:AEB12962.1};
OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Marinithermus.
OX NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB12962.1, ECO:0000313|Proteomes:UP000007030};
RN [1] {ECO:0000313|EMBL:AEB12962.1, ECO:0000313|Proteomes:UP000007030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX PubMed=22675595; DOI=10.4056/sigs.2435521;
RA Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J.,
RA Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT chimney.";
RL Stand. Genomic Sci. 6:21-30(2012).
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; CP002630; AEB12962.1; -; Genomic_DNA.
DR RefSeq; WP_013705006.1; NC_015387.1.
DR AlphaFoldDB; F2NRB3; -.
DR STRING; 869210.Marky_2242; -.
DR KEGG; mhd:Marky_2242; -.
DR eggNOG; COG2008; Bacteria.
DR HOGENOM; CLU_029381_0_2_0; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000007030; Chromosome.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:AEB12962.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007030}.
FT DOMAIN 5..285
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 200
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 341 AA; 36397 MW; 1B923E0EE2C5C8AC CRC64;
MRTIDLRSDT VTRPTPAMRR AMAEAEVGDD VYREDPTVNR LEALAAETLG CERAVFMPSG
TMTNQVALMV HLKRGAEVIA PEGAHIYEFE PGAIGVLSGG VPRLVPAPYG VPDLEALRRA
IHTSPHQAPT GLIALENTHN LAGGTVVPLE VQRKVQEIAR TAGLPTHLDG ARLFNAATYL
KVPAREVAAG FDTVSVCLSK GLGAPVGSLL LLPKALEPEA RRYRKMLGGG MRQAGVLAAA
GIVALQEGPA HLERDHQMAR ALAEGLVRLG LGVDLKAVQT NMVYARVPEA PRFVARLAAL
GVRANALGTD RVRFVTHRDL DDADIPQALE RIAQALERTS A
//
