ID I0HIU2_ACTM4 Unreviewed; 427 AA.
AC I0HIU2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative threonine synthase {ECO:0000313|EMBL:BAL92929.1};
GN OrderedLocusNames=AMIS_77090 {ECO:0000313|EMBL:BAL92929.1};
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL92929.1, ECO:0000313|Proteomes:UP000007882};
RN [1] {ECO:0000313|EMBL:BAL92929.1, ECO:0000313|Proteomes:UP000007882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC NCIMB 12654 / NRRL B-3342 / UNCC 431
RC {ECO:0000313|Proteomes:UP000007882};
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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DR EMBL; AP012319; BAL92929.1; -; Genomic_DNA.
DR RefSeq; WP_014447812.1; NC_017093.1.
DR AlphaFoldDB; I0HIU2; -.
DR STRING; 512565.AMIS_77090; -.
DR KEGG; ams:AMIS_77090; -.
DR PATRIC; fig|512565.3.peg.7725; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_028142_4_1_11; -.
DR OrthoDB; 9778118at2; -.
DR Proteomes; UP000007882; Chromosome.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR CDD; cd01563; Thr-synth_1; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000007882}.
FT DOMAIN 85..394
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 123
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 427 AA; 44532 MW; 1DE4DDFA8AA82761 CRC64;
MTSAVSAPTA TPTSPARGLI CRACAAEYPL AAQHACYECF GPLEVAYDEA ALARVTRAEI
EAGPQNIWRY AALLPAGQDP ATRVTLDPGL TPLVSAPALA AAVGLTAPLW VKDDSQNPTH
SFKDRVVSVA LTAAQELGFK RFSCASTGNL ANSVAAHAAR AGVPSIVFIP SDLEQGKIIT
TAVYGGDLVA IEGSYDDVNR LCSELVETDE FEDTAFVNVN VRPFYAEGSK TLGYEVAEQL
GWRIPAQVVV PMASGELLTK IDKAFSELVE IGLVEAPEGG WTVFGAQSAG CNPIATALHN
DTDVITPVKP TGIAKSLNIG DPAAGPYAIE AVKRTGGWMD YADDEEIRAG IRLLAETTGI
FAETAGGTTV AVLKKLVEAG KLDPAKETVV YNTGEGLKTL DAVAGQVGPT HTIKPSLRGA
REAGLLG
//
