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Database: UniProt
Entry: D5ECD8_AMICL
LinkDB: D5ECD8_AMICL
Original site: D5ECD8_AMICL 
ID   D5ECD8_AMICL            Unreviewed;       373 AA.
AC   D5ECD8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:ADE56220.1};
GN   OrderedLocusNames=Amico_0072 {ECO:0000313|EMBL:ADE56220.1};
OS   Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC   Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC   Aminobacterium.
OX   NCBI_TaxID=572547 {ECO:0000313|EMBL:ADE56220.1, ECO:0000313|Proteomes:UP000002366};
RN   [1] {ECO:0000313|EMBL:ADE56220.1, ECO:0000313|Proteomes:UP000002366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12261 / ALA-1 {ECO:0000313|Proteomes:UP000002366};
RX   PubMed=21304712;
RA   Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA   Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Aminobacterium colombiense type strain (ALA-
RT   1).";
RL   Stand. Genomic Sci. 2:280-289(2010).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP001997; ADE56220.1; -; Genomic_DNA.
DR   RefSeq; WP_013047486.1; NC_014011.1.
DR   AlphaFoldDB; D5ECD8; -.
DR   STRING; 572547.Amico_0072; -.
DR   KEGG; aco:Amico_0072; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_028142_4_0_0; -.
DR   OrthoDB; 9778118at2; -.
DR   Proteomes; UP000002366; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
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:UP000002366}.
FT   DOMAIN          64..360
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   373 AA;  41006 MW;  CCA4402451E6CEDA CRC64;
     MLLCERCHQQ HEEDSKYWRC PCGGALLLHV DETRFPSQEA LQSRPSSLWR YKEALPLRDG
     TIPVSLGEGL TPLVPLPWKS GRVFFKLDYL CPTGSYKDRG VAYEVTRLKE LGISSIVEDS
     SGNAGAAMAA YAARAGIHCQ IFVPEYTSAG KCVQIESYGA ELVRVPGSRE DTTRAAEQAA
     SHTYYASHNW SPYFVHGIKT YAFEIWEQLQ CTAPHKIIVP AGQGSLVLGC YLAFRHLLQS
     KIISRFPQII AVQAKNCAPL YEAFIQRKEE PVQIEKQETI AEGISSALPV RGREVLAAIR
     KTGGEMLAVD EEEIKRGFYD LAKAGLYVEP TSAVVAAALA KLEGQGKLLT SETTVAFLSG
     SGLKATDKIL HLK
//
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