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Database: UniProt
Entry: A0A0J1H6W0_9GAMM
LinkDB: A0A0J1H6W0_9GAMM
Original site: A0A0J1H6W0_9GAMM 
ID   A0A0J1H6W0_9GAMM        Unreviewed;       805 AA.
AC   A0A0J1H6W0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   16-JAN-2019, entry version 21.
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:KLV07480.1};
GN   ORFNames=ABT56_05295 {ECO:0000313|EMBL:KLV07480.1};
OS   Photobacterium aquae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=1195763 {ECO:0000313|EMBL:KLV07480.1, ECO:0000313|Proteomes:UP000036097};
RN   [1] {ECO:0000313|EMBL:KLV07480.1, ECO:0000313|Proteomes:UP000036097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12159 {ECO:0000313|EMBL:KLV07480.1,
RC   ECO:0000313|Proteomes:UP000036097};
RA   Machado H., Gram L.;
RT   "Photobacterium galathea sp. nov.";
RL   Submitted (MAY-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KLV07480.1}.
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DR   EMBL; LDOT01000005; KLV07480.1; -; Genomic_DNA.
DR   RefSeq; WP_047877821.1; NZ_LDOT01000005.1.
DR   EnsemblBacteria; KLV07480; KLV07480; ABT56_05295.
DR   PATRIC; fig|1195763.3.peg.1121; -.
DR   OrthoDB; 1067792at2; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000036097; Unassembled WGS sequence.
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   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR001341; Asp_kinase.
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   TIGRFAMs; TIGR00657; asp_kinases; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000036097};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:KLV07480.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:KLV07480.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:KLV07480.1}.
FT   DOMAIN        7    278       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   DOMAIN      459    593       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      602    797       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
FT   COILED      706    726       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   805 AA;  87854 MW;  A9102978FC0530F1 CRC64;
     MSGRVERQLH KFGGSSLADA ECYRRVVAIV GEYAGEQDLV VVSAAGKTTN NLIEWMAQLE
     QDGRRAHETF QELRAFQQQL IEELLSGEPA DALLTQLHLE LSELVQLGDR PLSTAERAWV
     LGHGEQWSAR LLAALLSQSG LVASCLDSRT FLRAERAAQP EVDRALSWPL LQTQLAQQQH
     RVVITGFVAG NQAGETVLLG RNGSDYSATV IGALAGVGRV TIWSDVAGVY SADPHKVGDA
     CLLPLLRLDE ADELARLAAP VLHSRTLQPV ANSAIDLTLR CSHQPESGST RIERVLASGR
     GAKIVTSLEE VCLLEVQCPR AHLLEPMVAE LERLLLRAQL APLARDIQTD KGLIRLAYTS
     EIAGGVLALL QDSGIGVDLK LREGFSLVAA VGAGVVANAV HCHGFYQQLK REPVEFMTES
     ESGLSLVAVL RQTRLDDLIG RLHQQLFQAQ KRLGLVLCGK GNIGSRWLAL FEREKASIEK
     RHGMSFTLIG VVDSRQYWID TEGIEPQRVL DAFGDESVEY PPGDWLTELS GHGYDDVIVL
     DVTASEELAG RYPAIAEAGL HLISANKVAG SAAGDDYHAV IDAFAKSSRY WLYNATVGAG
     LPINHTVRDL SESGDTIIAL SGIFSGTLSW LFQQYDGSIP FSVLVEQAWQ QGLTEPDPRH
     DLDGSDVMRK LVILARESGL ELEPEQVKVE DLVPEAMRNL TLDGFFEQAE LLDAALSERL
     RKAQREDKVL RYVARLDRHG KAVVGVEALS AEHALANLLP CDNIFAIESH WYRDNPLVIR
     GPGAGRDVTA GALLSDINRM ATMLK
//
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