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Database: UniProt
Entry: A0A178K9T2_9GAMM
LinkDB: A0A178K9T2_9GAMM
Original site: A0A178K9T2_9GAMM 
ID   A0A178K9T2_9GAMM        Unreviewed;       819 AA.
AC   A0A178K9T2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   08-MAY-2019, entry version 20.
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=thrA {ECO:0000313|EMBL:OAN14130.1};
GN   ORFNames=A3K86_11110 {ECO:0000313|EMBL:OAN14130.1};
OS   Photobacterium jeanii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=858640 {ECO:0000313|EMBL:OAN14130.1, ECO:0000313|Proteomes:UP000078503};
RN   [1] {ECO:0000313|EMBL:OAN14130.1, ECO:0000313|Proteomes:UP000078503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-40508 {ECO:0000313|EMBL:OAN14130.1,
RC   ECO:0000313|Proteomes:UP000078503};
RA   Li Y.;
RT   "Photobacterium proteolyticum sp. nov. a protease producing bacterium
RT   isolated from ocean sediments of Laizhou Bay.";
RL   Submitted (MAR-2016) 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:OAN14130.1}.
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DR   EMBL; LVHF01000025; OAN14130.1; -; Genomic_DNA.
DR   RefSeq; WP_068330968.1; NZ_PYMD01000003.1.
DR   EnsemblBacteria; OAN14130; OAN14130; A3K86_11110.
DR   BioCyc; GCF_001650345:A3K86_RS11110-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000078503; 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   CDD; cd04257; AAK_AK-HSDH; 1.
DR   Gene3D; 3.40.1160.10; -; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR041743; AK-HSDH_N.
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; PF01842; ACT; 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; PS51671; ACT; 2.
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:UP000078503};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:OAN14130.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078503};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727}.
FT   DOMAIN      320    395       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      401    473       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   819 AA;  88100 MW;  5A9B68D921F2341F CRC64;
     MRVLKFGGSS LADADRFSRA AEIIANNARQ GEVSVVLSAP GKVTNKLVSV IDNTVANGEA
     ELQLADLEQV FQTLFADLKA LEPNLDKALL DGKLASSLGQ LKQYVHGIKL LGLCPDNVYA
     KMISKGERLS IVAMKAMLEA KGLKGFLIDP VEYLLAHGDY LEAHVDIEVS TQNFARNPLP
     QGHVNIMPGF TAGNEKGELV TLGRNGSDYS AAVLAACLRA ECCEIWTDVD GVYSCDPRLV
     PDARQIKSLS YQEAMELSYF GASVLHPKTI APIAQFHIPC LIKNSFNPQG AGSLIGQDTG
     EDKLDIKGIT TLKDLTMVNV SGPGMKGMVG MASRVFGAMS LAGVSIVLIT QSSSEYSISF
     CIESEDKPAA QQALQDSFEL ELKEGLLEPV EFLDDVAIVT LVGDGMRTSR GIASRFFTSL
     AEVNVNIVAI AQGSSERAIS AVIPADKVSE SVKACHENLF NSQHFLDVFV VGVGGVGGEL
     VDQIQRQQRK LADKGIVIRV CGLANSRGML LDSSGLALDN WRDQMGQADQ SFALASLIQL
     VQRNHIINPV IIDCTSDQGI ADQYADFLSA GFHVITPNKK SNTASMAYYH QLRQAARATR
     RKFMYDTTVG AGLPVIENLQ NLLAAGDELS RFSGILSGSL SYIFGKLDDG MSFSEATTVA
     RNNGFTEPDP RDDLSGMDVA RKLLILARES GLALELDDVE VEQALPPGFD ASGSVDDFMA
     RLPEADAYFA KLSEQAASEG KVLRYVGEID QGQCKVKLAA VDGDDPMFKI KDGENALAFY
     SRYYQPIPLV LRGYGAGTEV TAAGVFADLM RTLGWKLGV
//
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