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Database: UniProt
Entry: A4N5X5_HAEIF
LinkDB: A4N5X5_HAEIF
Original site: A4N5X5_HAEIF 
ID   A4N5X5_HAEIF            Unreviewed;       217 AA.
AC   A4N5X5;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Homoserine kinase {ECO:0000313|EMBL:EDJ90405.1};
DE            EC=2.7.1.39 {ECO:0000313|EMBL:EDJ90405.1};
GN   ORFNames=CGSHi22421_01647 {ECO:0000313|EMBL:EDJ90405.1};
OS   Haemophilus influenzae R3021.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=375432 {ECO:0000313|EMBL:EDJ90405.1, ECO:0000313|Proteomes:UP000003798};
RN   [1] {ECO:0000313|EMBL:EDJ90405.1, ECO:0000313|Proteomes:UP000003798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R3021 {ECO:0000313|EMBL:EDJ90405.1,
RC   ECO:0000313|Proteomes:UP000003798};
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; AAZE01000015; EDJ90405.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4N5X5; -.
DR   Proteomes; UP000003798; Unassembled WGS sequence.
DR   GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1100; -; 1.
DR   Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR029144; Thr_synth_N.
DR   InterPro; IPR037158; Thr_synth_N_sf.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR43515; THREONINE SYNTHASE-LIKE 1; 1.
DR   PANTHER; PTHR43515:SF1; THREONINE SYNTHASE-LIKE 1; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF14821; Thr_synth_N; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EDJ90405.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Transferase {ECO:0000313|EMBL:EDJ90405.1}.
FT   DOMAIN          10..78
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          86..160
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   217 AA;  23889 MW;  3DCB8549CD346224 CRC64;
     MNLYNIKHPE EQVTFSQAVR QGLGRDQGLF FPEVIPKLNN INELLELPLV ERSQKILGAL
     IDGELPQATL DAMVKNAFTF TAPLEKVEDN IYALELFHGP TLAFKDFGGR FMAQALAAVR
     GDGKITILTA TSGDTGAAVA HAFYGLENIN VVILYPKGKI SPLQEKLFCT LGGIFVLLRL
     TLISMRVRLW LSKPLMMLNC AKLSGLTLQI LLISAVY
//
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