ID A0A0D3HHP5_9ORYZ Unreviewed; 1675 AA.
AC A0A0D3HHP5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
OS Oryza barthii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART11G01710.1};
RN [1] {ECO:0000313|EnsemblPlants:OBART11G01710.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART11G01710.1};
RX DOI=10.1007/s12284-009-9025-z;
RA Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA Knight J., Niazi F., Egholm M., Wing R.A.;
RT "De novo next generation sequencing of plant genomes.";
RL Rice 2:35-43(2009).
RN [2] {ECO:0000313|EnsemblPlants:OBART11G01710.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NADP(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADPH; Xref=Rhea:RHEA:15761, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000256|RuleBase:RU000579};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC pathway; L-homoserine from L-aspartate: step 3/3.
CC {ECO:0000256|RuleBase:RU000579}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|RuleBase:RU000579}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000256|RuleBase:RU004171}.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000256|ARBA:ARBA00010199}.
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DR STRING; 65489.A0A0D3HHP5; -.
DR PaxDb; 65489-OBART11G01710-1; -.
DR EnsemblPlants; OBART11G01710.1; OBART11G01710.1; OBART11G01710.
DR Gramene; OBART11G01710.1; OBART11G01710.1; OBART11G01710.
DR eggNOG; KOG0455; Eukaryota.
DR eggNOG; KOG1347; Eukaryota.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000026960; Chromosome 11.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; 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 GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd13132; MATE_eukaryotic; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001342; HDH_cat.
DR InterPro; IPR019811; HDH_CS.
DR InterPro; IPR045069; MATE_euk.
DR InterPro; IPR002528; MATE_fam.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR11206; MULTIDRUG RESISTANCE PROTEIN; 1.
DR PANTHER; PTHR11206:SF102; PROTEIN DETOXIFICATION 20-RELATED; 1.
DR Pfam; PF00742; Homoserine_dh; 1.
DR Pfam; PF01554; MatE; 5.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 {ECO:0000256|RuleBase:RU000579};
KW Isoleucine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methionine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW NADP {ECO:0000256|RuleBase:RU000579};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000579};
KW Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW Threonine biosynthesis {ECO:0000256|RuleBase:RU000579};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 52..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 378..400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 700..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 730..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 766..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 861..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..948
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1013..1033
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1092..1116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1122..1143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1349..1547
FT /note="Homoserine dehydrogenase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00742"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1555..1616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1675 AA; 182789 MW; 93190D94CEC6ADA0 CRC64;
MERPGDEHDD CRTVPLLEPK HAHGEGSNDK QEEDEEEVGS LGRRVLVESK KLWVVAGPSI
CARFSTFGVT VISQAFIGHI GATELAGYAL VSTVLMRFSG GILCIGNIVW QSYGAKQYHM
LGIYLQRSWI VLLCCAVLLL PIYLFTTPLL IFLGQDPKIA AMAGTISLWX IPVMISNVGN
FTLQMDLQAQ SKNMIVTYLA MLNLGLHLFL SWLLTVQFYL GLAGVMGSML AFVFFGDCPL
TWTGFSSAAF TELGAIVKLS LSSGVMLCLN INGWEMISIG FLSATGVRVA NELGAGSARR
AKFAIFNVVT TSFSIGFMLF VLFLIFRGRL AYIFTESTVV ADAVAELSPL LAFSNLLNSI
QPMLSGVAYG SGWQSVVAYV NVTSYYLFGI PIGVILGYVL GFQVKGIWIG MLLGTLVQTI
VLLFITLRTD WEKQVEIARQ RLNRWSMDEN GRQQNPEHAY ACIKMEKPGD DEKLTVPLLE
PKPATNKHQE DDDAEEDEVG SVRQRVVEEN KKLWVVAGPS ICARFSSFGV TVISQAFIGH
IGATELAAYA LVSTVLMRFS NGILSRVAME RTTEDDERPT VPLLEPKPAI NGGGGGSNEE
EEEVGSLGRR LVEENKKLWV VAGPSICARA TSFGVTIVSQ AFIGHIGATE LAAYALVSTV
LMRLSVGILI GMASALETLC GQSYGAKQYH MLGIYLQRSW IVLFCCAVIL LPIYLFTTPL
LIALGQDPDI SVVAGTISLW YIPIMFSYVW GLTIQMYLQS QSKNMIVTYL SLLNFGLNLF
LSWLMVVKFH LGLAGVMGSX IGMASALETL CGQSYGAKQY HMLGIYLQRS WIVLFCCAVI
LLPIYLFTTP LLIALGQDPD ISVVAGTISL WYIPIMFSYV WGLTIQMYLQ SQSKNMIVTY
LSLLNFGLNL FLSWLMVVKF HLGLAGVMGS MVIACWIPIF GQLAYVFFGG CPQTWTGFSS
SAFTDLGAII KLSISSGVML CVELWYNTIL VLLTGYMKNA EVALDALSIC LNINGWEMMI
AIGFLAATGV RVANELGAGS ARRANLAYIF TESQEVVDAV ADLAPLLAFS ILLNSVQPVL
SGVAIGSGWQ SVVAYVNVAS YYLIGIPIGA ILGYALGFEV KGIWIGMLVG TLVQTLVLLF
ITLRTNWEKQ VEIALERLNR WYTDDNVKLS STQMAAPVRS VLPVVLLGCG GVGRHLLRHI
VSCRPLHANQ GVAIRVLGVA DSSSLLVADD LHSNGFDDAL LADLCAAKSA GSPLSSLLAR
GQCQLFNNTE ARRKVIDTAS VLGKTTGLVL VDCSATYDTV GMLKDAVDCG CCVVLANKKP
LTCAYEDFEK LVSNFRRIRF ESTVGAGLPV IASVTRIIAS GDPVSRIVGS LSGTLGYVMS
ELEDGKKFSE VVKTAKSLGY TEPDPRDDLS GMDVARKALI LARLLGQQIS MENINVESLY
PSELGPDAMS TKDFLESGLV QLDKSIEERV KAASLKGNVL RYVCKIESTG CQVGLEELPK
NSALGRLRGS DNVVEIYSRC YESAPLVIQG AGAGNDTTAA GVKAEVVQNR SPIQCKDQEP
LEPETKLKRR SNRDKPSFNQ EASAFEIFVD EDEPNKSGPS KLQDKNMKQD NPKLSQQASA
FEIFVDEDDP YCNNQKMVQH RHFNKENTQG YRLQTRKKFY IKTTTATLGE IHIEP
//
