(data stored in SCRATCH zone)

SWISSPROT: C3MHL1_SINFN

ID   C3MHL1_SINFN            Unreviewed;       465 AA.
AC   C3MHL1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 51.
DE   SubName: Full=Threonine synthetase protein {ECO:0000313|EMBL:ACP24339.1};
DE            EC=4.2.3.1 {ECO:0000313|EMBL:ACP24339.1};
GN   Name=thrC {ECO:0000313|EMBL:ACP24339.1};
GN   OrderedLocusNames=NGR_c05430 {ECO:0000313|EMBL:ACP24339.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24339.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24339.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR604450-51};
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DR   EMBL; CP001389; ACP24339.1; -; Genomic_DNA.
DR   RefSeq; WP_012707124.1; NC_012587.1.
DR   RefSeq; YP_002825092.1; NC_012587.1.
DR   STRING; 394.NGR_c05430; -.
DR   EnsemblBacteria; ACP24339; ACP24339; NGR_c05430.
DR   GeneID; 7791769; -.
DR   KEGG; rhi:NGR_c05430; -.
DR   PATRIC; fig|394.7.peg.3357; -.
DR   eggNOG; ENOG4105D98; Bacteria.
DR   eggNOG; COG0498; LUCA.
DR   HOGENOM; HOG000230745; -.
DR   KO; K01733; -.
DR   OMA; DIFILHP; -.
DR   OrthoDB; POG091H02AJ; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1380.10; -; 1.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR029144; Thr_synth_N.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR001926; TrpB-like_PLP-dep.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00260; thrC; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   4: Predicted;
DR   PRODOM; C3MHL1.
DR   SWISS-2DPAGE; C3MHL1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Lyase {ECO:0000313|EMBL:ACP24339.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN        2     80       Thr_synth_N. {ECO:0000259|Pfam:PF14821}.
FT   DOMAIN       98    399       PALP. {ECO:0000259|Pfam:PF00291}.
FT   MOD_RES     112    112       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|PIRSR:PIRSR604450-51}.
SQ   SEQUENCE   465 AA;  50849 MW;  0DBFFBE8256E5551 CRC64;
     MKYISTRGEA APLGFCDALL AGLARDGGLY LPKEWPTFSK KEIRALRGKS YQEIAFTVLQ
     PFTNGEIPAA KFREMIDGAY ATFRHPAIAP LVQTGPNAFV MELFHGSTLA FKDVAMQLLA
     RLMDHVLAER GERATIVGAT SGDTGGAAID AFAGRDRTDI FILFPHGKVS PVQQRQMTTA
     NASNVHAIAV NGNFDDCQNL VKAMFNDTAF RDRVKLSGVN SINWARIMAQ IVYYFTTAIA
     LGGPDRKISF TVPTGNFGDI FAGYVAKRMG LPIDKLIIAT NENDILARTL KTGRYEMREV
     KATTSPSMDI QISSNFERLL FEAFGREASE VRAAMASLKQ SGSFAIEEGA LKKIRKEFRA
     GRASEKQVAA TIRDTFKKSG YLLDPHTAIG VSVAAKHEKP SAPMVVLGTA HPAKFPDAVK
     SASGIDPTLP TWLADLMTRA ERFDILDAEL KNVETFIGER TRVQK
//

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