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Database: UniProt
Entry: F7NGB3_9FIRM
LinkDB: F7NGB3_9FIRM
Original site: F7NGB3_9FIRM 
ID   F7NGB3_9FIRM            Unreviewed;       431 AA.
AC   F7NGB3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   16-JAN-2019, entry version 38.
DE   RecName: Full=Homoserine dehydrogenase {ECO:0000256|RuleBase:RU000579};
DE            EC=1.1.1.3 {ECO:0000256|RuleBase:RU000579};
GN   ORFNames=ALO_05483 {ECO:0000313|EMBL:EGO64906.1};
OS   Acetonema longum DSM 6540.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Acetonema.
OX   NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO64906.1, ECO:0000313|Proteomes:UP000003240};
RN   [1] {ECO:0000313|EMBL:EGO64906.1, ECO:0000313|Proteomes:UP000003240}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO64906.1,
RC   ECO:0000313|Proteomes:UP000003240};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
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:EGO64906.1}.
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DR   EMBL; AFGF01000041; EGO64906.1; -; Genomic_DNA.
DR   RefSeq; WP_004093605.1; NZ_AFGF01000041.1.
DR   STRING; 1009370.ALO_05483; -.
DR   EnsemblBacteria; EGO64906; EGO64906; ALO_05483.
DR   eggNOG; ENOG4105D6E; Bacteria.
DR   eggNOG; COG0460; LUCA.
DR   OrthoDB; 1464088at2; -.
DR   BioCyc; ALON1009370:G10BF-3528-MONOMER; -.
DR   UniPathway; UPA00050; UER00063.
DR   UniPathway; UPA00051; UER00465.
DR   Proteomes; UP000003240; 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; IPR002912; ACT_dom.
DR   InterPro; IPR005106; Asp/hSer_DH_NAD-bd.
DR   InterPro; IPR016204; HDH.
DR   InterPro; IPR001342; HDH_cat.
DR   InterPro; IPR019811; HDH_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00742; Homoserine_dh; 1.
DR   Pfam; PF03447; NAD_binding_3; 1.
DR   PIRSF; PIRSF000098; Homoser_dehydrog; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51671; ACT; 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:UP000003240};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW   NADP {ECO:0000256|PIRSR:PIRSR000098-2, ECO:0000256|RuleBase:RU000579};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000579,
KW   ECO:0000313|EMBL:EGO64906.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003240};
KW   Threonine biosynthesis {ECO:0000256|RuleBase:RU000579}.
FT   DOMAIN      350    424       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   NP_BIND      10     17       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   ACT_SITE    205    205       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR000098-1}.
FT   BINDING     105    105       NADP. {ECO:0000256|PIRSR:PIRSR000098-2}.
FT   BINDING     190    190       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000098-2}.
SQ   SEQUENCE   431 AA;  46892 MW;  65B5591C4B9E568A CRC64;
     MKETVQIGLL GYGTVGTGII KILQTNAHNI AQKVGCPLAI KKVLVRNPGK TRNTSFNVPL
     TTSIDEILND PDIDIVVEVM GGESPAKDYI LRALEAGKHV VTANKDIIAK YGKQLFEAAE
     EKQVDLLFEA SVGGGIPIIR PLKQCLAANR IREVMGIVNG TTNYMLTKMT QERLDFETVL
     AEAQAKGYAE ADPTADIGGW DAARKIAILA SIAFNSRITL DDVQVEGIEN ISPDDIEYAR
     ELGYAVKLLA IAKESESGID VRVHPTLLPH HHPLASVNDV FNAIYVRGDA VGETMFYGRG
     AGEMPTASAA VADIIDAARD IRHHVSSRIL CTCFNQKNLS SAQHTESPFY IRLLVEDRPG
     ALAVIAGAFG AQQVSLHSVI QKRRINNFAE LVLITHKVPY ASIKLAINTM EDMSVVRKVH
     NVIHVEAGEF E
//
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