GenomeNet

Database: UniProt
Entry: Q15PV6_PSEA6
LinkDB: Q15PV6_PSEA6
Original site: Q15PV6_PSEA6 
ID   Q15PV6_PSEA6            Unreviewed;       820 AA.
AC   Q15PV6;
DT   25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   25-JUL-2006, sequence version 1.
DT   03-JUL-2019, entry version 97.
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   OrderedLocusNames=Patl_3580 {ECO:0000313|EMBL:ABG42082.1};
OS   Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=342610 {ECO:0000313|EMBL:ABG42082.1, ECO:0000313|Proteomes:UP000001981};
RN   [1] {ECO:0000313|EMBL:ABG42082.1, ECO:0000313|Proteomes:UP000001981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T6c / ATCC BAA-1087 {ECO:0000313|Proteomes:UP000001981};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Karls A.C., Bartlett D., Higgins B.P., Richardson P.;
RT   "Complete sequence of Pseudoalteromonas atlantica T6c.";
RL   Submitted (JUN-2006) 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; CP000388; ABG42082.1; -; Genomic_DNA.
DR   RefSeq; WP_011576307.1; NC_008228.1.
DR   STRING; 342610.Patl_3580; -.
DR   EnsemblBacteria; ABG42082; ABG42082; Patl_3580.
DR   KEGG; pat:Patl_3580; -.
DR   eggNOG; ENOG4105CFH; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   eggNOG; COG0527; LUCA.
DR   HOGENOM; HOG000271593; -.
DR   KO; K12524; -.
DR   OMA; CNKIACS; -.
DR   OrthoDB; 1067792at2; -.
DR   BioCyc; PATL342610:G1G6R-3706-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000001981; 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; 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:UP000001981};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:ABG42082.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:ABG42082.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001981};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:ABG42082.1}.
FT   DOMAIN      320    394       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      401    483       ACT. {ECO:0000259|PROSITE:PS51671}.
SQ   SEQUENCE   820 AA;  88688 MW;  B65BA3642EB9A8C1 CRC64;
     MKVLKFGGSS LADAERYLRV KDICLDTHAS NGAAVVLSAP KGVTNALSLL CEEAGSGKDY
     GELFAKLNMV LFGILDDLKD TLPEFDDSEL APYIQRILNE LNQHLEGFAL LRCAPESVVA
     KILSIGEYMS VNIFSQILTT LGTKNQIIDP AELILAEGDY LDSIADVAVS KARFSDVDSS
     GDVVLIMPGF VAVNAEGEKV TLGRNGSDYS AAILAACIDA ECCEIWTDVD GVYNADPNQV
     DGAVLLDKLT YQEAMELSYF GAKVLHPKTI GPIAQHHIPC LIRNTLNPAA PGTLISNEKS
     TKWTSVKGIS HLDDMTMFNV AGPGMKGMVG MASRVFEVMS NANISISLIT QSSSEYSISF
     CIHSKDATRA QDLLEDSFAL ELANNLLDPI EVRHDLAIVT LVGDGMRHSQ GLAAKFFSSL
     AQARVNNVAI AQGSSERSIS TVIESSKARK AVKVVHQNFF SNLHAIDVFL VGCGTVGKEL
     LGQIARQQAV LLERGISLKI YGIANSRKLL LEAGGVDLSA DWTSQLNASE QSLSVDALQN
     FVMRNSLVNP VVIDCTSSTV IAELYVELMN SGFHVVTPNK KANTASYAYY QQLRETAQNT
     NRQFLYETTV GAGLPVIDNL QKLIYAGDEL QRFEGILSGS LSFVFGKLDE GLTLSQATEI
     AKKNGFTEPD PRDDLSGTDV ARKLLIMARE ADLKLELEDI QIEPVLPSHF DDSGSIDEFM
     AKLPELDALY TDKVNAAKEE GKVLRYVGSI SKGKCVVSIQ AVGEDHPLFV IKEGENALAI
     HSNYYQPIPY VIRGYGAGAA VTAAGVFADV LRTMPWKQDV
//
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