ID D2PP37_KRIFD Unreviewed; 401 AA.
AC D2PP37;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN OrderedLocusNames=Kfla_5627 {ECO:0000313|EMBL:ADB34633.1};
OS Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB34633.1, ECO:0000313|Proteomes:UP000007967};
RN [1] {ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Pukall R., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Kribbella flavida DSM 17836.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADB34633.1, ECO:0000313|Proteomes:UP000007967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC {ECO:0000313|Proteomes:UP000007967};
RX PubMed=21304701;
RA Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., LaButti K., Pati A., Ivanova N.,
RA Mavrommatis K., Mikhailova N., Pitluck S., Bruce D., Goodwin L., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C.D., Chen A., Palaniappan K., Chain P.,
RA Rohde M., Goeker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P., Brettin T.;
RT "Complete genome sequence of Kribbella flavida type strain (IFO 14399).";
RL Stand. Genomic Sci. 2:186-193(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP001736; ADB34633.1; -; Genomic_DNA.
DR RefSeq; WP_012923187.1; NC_013729.1.
DR AlphaFoldDB; D2PP37; -.
DR STRING; 479435.Kfla_5627; -.
DR KEGG; kfl:Kfla_5627; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_1_11; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000007967; Chromosome.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR CDD; cd04886; ACT_ThrD-II-like; 1.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR044561; ACT_ThrD-II-like.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR005789; Thr_deHydtase_catblc.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01127; ilvA_1Cterm; 1.
DR PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 4: Predicted;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000007967}.
FT DOMAIN 18..303
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 401 AA; 41978 MW; A7DE67EE4455ED5D CRC64;
MSISAAEIAR AADLLHDVVA PTPLEYSRWL SELVGGDVFL KCENLQRTGS FKLRGAYVRM
ARLTKKERAR GVVAASAGNH AQGVALAAQL LGIKATVFMP HGAPIPKEKA TRAYGAQIRF
VGTSIDECLA SAREFEAETG AILIHPFDHP DIVAGQATTG LEIVEQCPQV RTVVVPTGGG
GLVAGIASAM QRDGMPISVV GVQAAGAAAY PASLAAGAPV ALATMSTMAD GIAVGLPGQV
PFAAIQAHVG EILTVGEDSL SKALLLVLER AKLVVEPAGA AAVAAVLDDP LRFKPPVVVV
LSGGNIDPVL LMRVLRHGMA AAGRYLSLRV RIPDTPGGLA SLLTRLAEVE ANIIEVLHER
ISETLNLDEV EVALQLETRG EEHRMRVLTS LTSHGYTYTL N
//
