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Database: UniProt
Entry: A0A0F7H8R6_SERFO
LinkDB: A0A0F7H8R6_SERFO
Original site: A0A0F7H8R6_SERFO 
ID   A0A0F7H8R6_SERFO        Unreviewed;       811 AA.
AC   A0A0F7H8R6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   03-JUL-2019, entry version 22.
DE   RecName: Full=Bifunctional aspartokinase/homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE   Includes:
DE     RecName: Full=Aspartokinase {ECO:0000256|PIRNR:PIRNR000727};
DE              EC=2.7.2.4 {ECO:0000256|PIRNR:PIRNR000727};
DE   Includes:
DE     RecName: Full=Homoserine dehydrogenase {ECO:0000256|PIRNR:PIRNR000727};
DE              EC=1.1.1.3 {ECO:0000256|PIRNR:PIRNR000727};
GN   Name=metL {ECO:0000313|EMBL:AKG68896.1};
GN   ORFNames=WN53_06995 {ECO:0000313|EMBL:AKG68896.1};
OS   Serratia fonticola.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG68896.1, ECO:0000313|Proteomes:UP000034699};
RN   [1] {ECO:0000313|EMBL:AKG68896.1, ECO:0000313|Proteomes:UP000034699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG68896.1,
RC   ECO:0000313|Proteomes:UP000034699};
RA   Chan K.-G., Ee R.;
RT   "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP;
CC         Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000727};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-
CC         semialdehyde + NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57476, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:537519; EC=1.1.1.3;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000727};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
CC       {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the homoserine
CC       dehydrogenase family. {ECO:0000256|PIRNR:PIRNR000727}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       aspartokinase family. {ECO:0000256|PIRNR:PIRNR000727}.
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DR   EMBL; CP011254; AKG68896.1; -; Genomic_DNA.
DR   RefSeq; WP_024482870.1; NZ_CP011254.1.
DR   EnsemblBacteria; AKG68896; AKG68896; WN53_06995.
DR   KEGG; sfw:WN53_06995; -.
DR   PATRIC; fig|47917.8.peg.1451; -.
DR   KO; K12525; -.
DR   OMA; GAGVCKN; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000034699; Chromosome.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniRule.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd04257; AAK_AK-HSDH; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR041743; AK-HSDH_N.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   InterPro; IPR011147; Bifunc_aspartokin/hSer_DH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000727; ThrA; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR000727};
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034699};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:AKG68896.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:AKG68896.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:AKG68896.1}.
FT   DOMAIN       13    285       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   DOMAIN      466    601       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      609    804       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
SQ   SEQUENCE   811 AA;  88858 MW;  F449A8906744DA02 CRC64;
     MNAIAVAGPV SGRQLHKFGG SSLADVKCYL RVAGIMAEYS QPGDMMVVSA AGSTTNQLIS
     WLKLSQSDRL SAHQVQQTLR RYHSELIGGL LPVETAEPLI AEFIHDLERL AILLDGKVDD
     AVYAEVVGHG EIWSARLMAA VLNKQDMQAA WLDARDFLRA ERAAQPQVDE GRSYPLLQQL
     LAQHPGKRLV VTGFISRNDS GETVLLGRNG SDYSATQVGA LAGVERVTIW SDVAGVYSAD
     PRKVKDACLL PLLRLDEASE LARLAAPVLH TRTLQPVSGS DIDLQLRCSY QPEQGSTRIE
     RVLASGTGAK IVTSHDDVCL IELSVAPQHD FKLAQKELDL VLKRAQIKPL AVGVHPDRNL
     IQLCYTSEVV GSVLRILQEA GLPGELQLRE GLALVALVGA GVCKNPLHSH RFYQQLKDQP
     VEFIWQAEDG ISLVAVLRQG PTGLLIQGLH QTLFRAEKRI GLVLFGKGNI GSRWLELFAR
     EQKNISARSG FEFSLAGVVD SRRSLLNYEG LDASRALAFF EDEAQELDEE SLFLWMRAHP
     FDDLVVLDVT ASGELAEQYL DFASYGFHVI SANKLAGASC SANYRQIRDA FAKTGRHWLY
     NATVGAGLPV NHTVRDLRDS GDSILAISGI FSGTLSWLFL QFDGTVPFTE LVDQAWQQGL
     TEPDPRVDLS GQDVMRKLVI LAREAGYDIE PNQVRVESLV PAGAEQGSID QFFENGDALN
     QQMLQRFEAA NEMGLVLRHV ARFDANGKAR VGVEAVRPEH PLASLLPCDN VFAIESRWYR
     DNPLVIRGPG AGRDVTAGAI QSDLNRLAQL L
//
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