ID C5CA62_MICLC Unreviewed; 440 AA.
AC C5CA62;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Homoserine dehydrogenase {ECO:0000256|ARBA:ARBA00013376, ECO:0000256|RuleBase:RU000579};
DE EC=1.1.1.3 {ECO:0000256|ARBA:ARBA00013213, ECO:0000256|RuleBase:RU000579};
GN Name=hom {ECO:0000313|EMBL:SQG49284.1};
GN OrderedLocusNames=Mlut_08020 {ECO:0000313|EMBL:ACS30331.1};
GN ORFNames=NCTC2665_01820 {ECO:0000313|EMBL:SQG49284.1};
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Micrococcus.
OX NCBI_TaxID=465515 {ECO:0000313|EMBL:ACS30331.1, ECO:0000313|Proteomes:UP000000738};
RN [1] {ECO:0000313|EMBL:ACS30331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCTC 2665 {ECO:0000313|EMBL:ACS30331.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Lowry S., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Young M., Greenblatt C.;
RT "Complete sequence of Micrococcus luteus NCTC 2665.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000000738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 /
RC NCTC 2665 / VKM Ac-2230 {ECO:0000313|Proteomes:UP000000738};
RX PubMed=19948807; DOI=10.1128/JB.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
RN [3] {ECO:0000313|EMBL:SQG49284.1, ECO:0000313|Proteomes:UP000248985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC2665 {ECO:0000313|EMBL:SQG49284.1,
RC ECO:0000313|Proteomes:UP000248985};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homoserine + NAD(+) = H(+) + L-aspartate 4-semialdehyde +
CC NADH; Xref=Rhea:RHEA:15757, ChEBI:CHEBI:15378, ChEBI:CHEBI:57476,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:537519; EC=1.1.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00001406};
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|ARBA:ARBA00000116,
CC 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|ARBA:ARBA00005062, ECO:0000256|RuleBase:RU000579}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC from L-aspartate: step 3/5. {ECO:0000256|ARBA:ARBA00005056,
CC ECO:0000256|RuleBase:RU000579}.
CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006753, ECO:0000256|RuleBase:RU004171}.
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DR EMBL; CP001628; ACS30331.1; -; Genomic_DNA.
DR EMBL; LS483396; SQG49284.1; -; Genomic_DNA.
DR RefSeq; WP_010079030.1; NZ_WBMF01000002.1.
DR AlphaFoldDB; C5CA62; -.
DR STRING; 465515.Mlut_08020; -.
DR EnsemblBacteria; ACS30331; ACS30331; Mlut_08020.
DR KEGG; mlu:Mlut_08020; -.
DR PATRIC; fig|465515.4.peg.765; -.
DR eggNOG; COG0460; Bacteria.
DR eggNOG; COG2716; Bacteria.
DR HOGENOM; CLU_009116_1_0_11; -.
DR UniPathway; UPA00050; UER00063.
DR UniPathway; UPA00051; UER00465.
DR Proteomes; UP000000738; Chromosome.
DR Proteomes; UP000248985; Chromosome 1.
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 CDD; cd04881; ACT_HSDH-Hom; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
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 PANTHER; PTHR43331; HOMOSERINE DEHYDROGENASE; 1.
DR PANTHER; PTHR43331:SF1; HOMOSERINE DEHYDROGENASE; 1.
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; SSF55021; ACT-like; 1.
DR SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 {ECO:0000256|RuleBase:RU000579};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624,
KW ECO:0000256|RuleBase:RU000579};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167,
KW ECO:0000256|RuleBase:RU000579};
KW NADP {ECO:0000256|PIRSR:PIRSR000098-2, ECO:0000256|RuleBase:RU000579};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000579};
KW Reference proteome {ECO:0000313|Proteomes:UP000000738};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW ECO:0000256|RuleBase:RU000579}.
FT DOMAIN 359..436
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-1"
FT BINDING 16..23
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 110
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000098-2"
SQ SEQUENCE 440 AA; 45372 MW; 3A11F79C42786833 CRC64;
MPQHTDAPTA LKVALLGGGT VGSQTARILT EDADILRDRV GADLELTGIA VRDTGATRDW
QADPALYTTD AEALVAGADV VIELMGGIEP ARTLILRALA AGTSVVTGNK ALLAQHGEEL
YAAAAATGAQ LSFEAAVAGA IPILRPLRDS LGGDRVTRVM GIANGTTNFI LDRMDSEGAD
FDDALAEAQR LGYAEADPTA DVEGHDAAAK AAILATIAFG APYTLDQVAV AGITAITAED
NAAAAEAGYV IKLLAIAERG RAADGAEGAV LRVHPTLLPR EHPLASVRGA FNAVFVEAEN
AGELMFYGPG AGGAPTASAV MGDVVSIAQR IVRGGPARLR TPVTALPALD PAEAHTSFMV
VLRAADQPGV LRRVAGVFEE HGVSIETLRQ VPSEREDAPG ASLRLITHRA RQRDLDATVE
ALAALDVVHE VASVLRVEGN
//
