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Database: UniProt
Entry: D2Z7Q5_9BACT
LinkDB: D2Z7Q5_9BACT
Original site: D2Z7Q5_9BACT 
ID   D2Z7Q5_9BACT            Unreviewed;       349 AA.
AC   D2Z7Q5;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   16-JAN-2019, entry version 39.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=Dpep_1476 {ECO:0000313|EMBL:EFC91502.1};
OS   Dethiosulfovibrio peptidovorans DSM 11002.
OC   Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC   Dethiosulfovibrio.
OX   NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC91502.1, ECO:0000313|Proteomes:UP000006427};
RN   [1] {ECO:0000313|EMBL:EFC91502.1, ECO:0000313|Proteomes:UP000006427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC91502.1,
RC   ECO:0000313|Proteomes:UP000006427};
RX   PubMed=21304695;
RA   Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Goodwin L., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans
RT   type strain (SEBR 4207).";
RL   Stand. Genomic Sci. 3:85-92(2010).
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|RuleBase:RU000579};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 3/3.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 3/5.
CC       {ECO:0000256|RuleBase:RU000579}.
CC   -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU004171}.
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:EFC91502.1}.
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DR   EMBL; ABTR02000001; EFC91502.1; -; Genomic_DNA.
DR   RefSeq; WP_005660934.1; NZ_ABTR02000001.1.
DR   STRING; 469381.Dpep_1476; -.
DR   EnsemblBacteria; EFC91502; EFC91502; Dpep_1476.
DR   eggNOG; ENOG4105D6E; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   OrthoDB; 1464088at2; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000006427; Unassembled WGS sequence.
DR   GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR022697; HDH_short.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF036497; HDH_short; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS01042; HOMOSER_DHGENASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU000579};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006427};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRSR:PIRSR036497-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000579,
KW   ECO:0000313|EMBL:EFC91502.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006427};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN        9    149       NAD_binding_3. {ECO:0000259|Pfam:
FT                                PF03447}.
FT   DOMAIN      157    334       Homoserine_dh. {ECO:0000259|Pfam:
FT                                PF00742}.
FT   ACT_SITE    224    224       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR036497-1}.
FT   BINDING     125    125       NADP. {ECO:0000256|PIRSR:PIRSR036497-2}.
FT   BINDING     209    209       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR036497-2}.
SQ   SEQUENCE   349 AA;  36779 MW;  A7E0861DD43D0254 CRC64;
     MELGIALVGF GNVAQGLARI LIRKRDLLTT RYGIIPVVKA VVTGSKGTLW DPSGLDLEAV
     LDSMADLENL SGVSALPATI DEILKGDEIS VVVDTTPTDL VTGEPGLSII KRAIESGKHV
     VSSSKGPVSV ALPELTDLAT RHGVAYRFEG ALLSGTPSIN LAMEAMAGCD VVKVQGIVNG
     TTNYILTRME EGMGYEDALA EAQDRGYAET DPSGDVDGWD AAVKAQIIAS VIMGEPISLD
     QVERRGISEI SRSDVLAALD RGNRIKLIAQ VERRGRDVVA SVSPMELPLD HPLAGVMGAT
     NAITYETDNL KDVTIVGPGA GREETGQALL ADLLAIFRER GGLVVRRSA
//
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