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Database: UniProt
Entry: A0A1S6HRG6_9GAMM
LinkDB: A0A1S6HRG6_9GAMM
Original site: A0A1S6HRG6_9GAMM 
ID   A0A1S6HRG6_9GAMM        Unreviewed;       795 AA.
AC   A0A1S6HRG6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   13-FEB-2019, entry version 13.
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   ORFNames=Sps_02955 {ECO:0000313|EMBL:AQS38102.1};
OS   Shewanella psychrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225848 {ECO:0000313|EMBL:AQS38102.1, ECO:0000313|Proteomes:UP000189545};
RN   [1] {ECO:0000313|EMBL:AQS38102.1, ECO:0000313|Proteomes:UP000189545}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP2 {ECO:0000313|EMBL:AQS38102.1,
RC   ECO:0000313|Proteomes:UP000189545};
RA   Xu G., Jian H.;
RT   "Complete genome sequence of Shewanella psychrophila WP2, a deep sea
RT   bacterium isolated from west Pacific sediment.";
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}.
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DR   EMBL; CP014782; AQS38102.1; -; Genomic_DNA.
DR   KEGG; spsw:Sps_02955; -.
DR   KO; K12525; -.
DR   BioCyc; GCF_002005305:SPS_RS14560-MONOMER; -.
DR   UniPathway; UPA00034; UER00015.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00462.
DR   Proteomes; UP000189545; 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   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; 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:UP000189545};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000727, ECO:0000313|EMBL:AQS38102.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000727};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000727};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000727};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000727,
KW   ECO:0000313|EMBL:AQS38102.1}.
FT   DOMAIN        7    276       AA_kinase. {ECO:0000259|Pfam:PF00696}.
FT   DOMAIN      444    565       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      587    785       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
SQ   SEQUENCE   795 AA;  87885 MW;  F7B103AF1CDCB411 CRC64;
     MARCHLHKFG GSSLADADCY RRVAHILLTH GNSDDLVVVS AAGKSTNFLY KLLELKDTGQ
     LWQEELQVLI SFQQNLIEQL LSNEQARSLR ERLSIDKYQL ISLFSLESLN EYKRSEVVSF
     GERWSARLLA ALLRESGVAA SDVDARSLLL ADEGGVPQIR LDESRSRVQK TLGEHPNERL
     IITGFICANS RGETLLLGRN GSDYSATLIA SLANIERVTI WTDVEGVFNA DPNKINDAKL
     LKSLSLDEAN RLAHLGSPVL HNRSLQPLFD TQVSLAVRSS YASHTDFTLI APKSSQASAP
     VVTNLSSVSL FSFRISSDTA NLAELLEVAG LIPLAHWKLA HNRVELAFTH ENQKQVQAIL
     ATDALEVSDI HIREDLGLVA LVSADAGLYR RGFARLLSRD ARPLFKDGLS LVTLVPTSQV
     NLLTQKVHRR CAGPRKRIGV LLLGVGNIGE TWARLFSRAR VALNKELEAS VELVGLLSSK
     KALLKEEGID LDSWKQAFDE QATPWLYDHM FEQLQALECD ELIALDISAS ADLTLQYPEF
     FSRGIHVVSA NKLAGSGPLA FYRELKLQLG NRRLFWRYNA SCGAGLPVQH ALNDLHNSGD
     SIEAVGGIFS GTLCWLFEKY DAKKPFSELV LEARGLGITE PDPRDDLSGR DMQRKLLILA
     REIGHEIELE DIELHSLVPA DLADIPLEQF LARISELDGD MLQQFQTAAE QSKVLRYVAG
     LDVVDGQLKA AVRMEWVDTQ HAYANLTPGD NVFVIRSAFY QDNPLIIRGP GAGREVTAAA
     VQSDLAQICR DLVQE
//
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