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Database: UniProt
Entry: F9RAT1_VIBSN
LinkDB: F9RAT1_VIBSN
Original site: F9RAT1_VIBSN 
ID   F9RAT1_VIBSN            Unreviewed;       819 AA.
AC   F9RAT1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   08-MAY-2019, entry version 36.
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:EGU34847.1};
GN   ORFNames=VIBRN418_07010 {ECO:0000313|EMBL:EGU34847.1};
OS   Vibrio sp. (strain N418).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU34847.1, ECO:0000313|Proteomes:UP000003627};
RN   [1] {ECO:0000313|EMBL:EGU34847.1, ECO:0000313|Proteomes:UP000003627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N418 {ECO:0000313|EMBL:EGU34847.1,
RC   ECO:0000313|Proteomes:UP000003627};
RA   Strain E.A., Brown E., Allard M.W.;
RL   Submitted (AUG-2011) 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:EGU34847.1}.
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DR   EMBL; AFWD01000039; EGU34847.1; -; Genomic_DNA.
DR   RefSeq; WP_009385774.1; NZ_AFWD01000039.1.
DR   STRING; 701176.VIBRN418_07010; -.
DR   EnsemblBacteria; EGU34847; EGU34847; VIBRN418_07010.
DR   eggNOG; ENOG4105CFH; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   eggNOG; COG0527; LUCA.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000003627; 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; IPR027795; CASTOR_ACT_dom.
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; PF13840; ACT_7; 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:UP000003627};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:EGU34847.1};
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:UP000003627};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:EGU34847.1}.
FT   DOMAIN      320    395       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      401    473       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   819 AA;  87959 MW;  016E38C5B24C9A31 CRC64;
     MRVLKFGGSS LADADRFLRA ADIVANNAQQ EEVAVVLSAP GKTTNKLVAV IEAALKSGDA
     ESQIAELEDA FRGLFEDIKQ VLPNIDGSGY NQQVKSSLSQ LRQFVNGIGL LGMCPDNVNA
     RIISKGERVS IQLMKAVLEA KGQPAHLIDP VEYLFARGEH LEAMVDVDIS TQNFRQKPLP
     QGHVNIMPGF TAGNEKGELV TLGRNGSDYS AAVLAACLRA DCCEIWTDVD GVYNCDPRLV
     ADARLLKSLS YQEAMELSYF GASVLHPKTI APIAQFHIPC LIKNSFNPQG AGTLIGQDTG
     EDKLAIKGIT TLSDLTMVNV SGPGMKGMVG MASRVFGAMS SSGVSIVLIT QSSSEYSISF
     CIEAQDKAIA QQALCDAFEL ELKDGLLEPV EYIDNVAIVT LVGDGMRTSR GVASQFFSSL
     AEVNVNIVAI AQGSSERAIS AVIPEDKISE AIKACHENLF NSKHFLDVFV VGVGGVGGEL
     VDQIQRQQAK LAEKGIVLRV CGLANSKGVL LDGEGLPLDH WRDRMNGVSE PLSLASLSSL
     VQRNHIINPV LVDCTSSEVI ANQYADFLAA GFHVVTPNKK ANTASMSYYH QLRDVARSSR
     RKLMYETTVG AGLPVIENLQ NLISAGDELE RFTGILSGSL SYIFGKLDEG MTLSQATNIA
     KDNGFTEPDP RDDLSGMDVA RKLLILAREA GMALELEDVI VDQALPPGFD DSGSVDEFMA
     RLPEADAYFQ QQVAQAAAEG KVLRYVGEIA NGQCRVSIAA VDENDPMFKI KDGENALAFF
     SRYYNPIPLV LRGYGAGTEV TAAGVFADVM RTLGWKLGV
//
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