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Database: UniProt
Entry: M2XYC0_9MICC
LinkDB: M2XYC0_9MICC
Original site: M2XYC0_9MICC 
ID   M2XYC0_9MICC            Unreviewed;       382 AA.
AC   M2XYC0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE            EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN   ORFNames=C884_01167 {ECO:0000313|EMBL:EME37793.1};
OS   Kocuria palustris PEL.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=1236550 {ECO:0000313|EMBL:EME37793.1, ECO:0000313|Proteomes:UP000009877};
RN   [1] {ECO:0000313|EMBL:EME37793.1, ECO:0000313|Proteomes:UP000009877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEL {ECO:0000313|EMBL:EME37793.1,
RC   ECO:0000313|Proteomes:UP000009877};
RX   PubMed=24504000;
RA   Sharma G., Khatri I., Subramanian S.;
RT   "Draft Genome Sequence of Kocuria palustris PEL.";
RL   Genome Announc. 2:e01261-13(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate 4-semialdehyde + NADP(+) + phosphate = 4-phospho-
CC         L-aspartate + H(+) + NADPH; Xref=Rhea:RHEA:24284, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57535, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:537519; EC=1.2.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001636};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00005076}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo
CC       pathway; L-homoserine from L-aspartate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00005021}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 2/5. {ECO:0000256|ARBA:ARBA00005097}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00010584}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EME37793.1}.
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DR   EMBL; ANHZ02000002; EME37793.1; -; Genomic_DNA.
DR   AlphaFoldDB; M2XYC0; -.
DR   STRING; 71999.KPaMU14_10115; -.
DR   UniPathway; UPA00034; UER00016.
DR   UniPathway; UPA00050; UER00463.
DR   UniPathway; UPA00051; UER00464.
DR   Proteomes; UP000009877; Unassembled WGS sequence.
DR   GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000319; Asp-semialdehyde_DH_CS.
DR   InterPro; IPR011534; Asp_ADH_gamma-type.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   NCBIfam; TIGR01745; asd_gamma; 1.
DR   PANTHER; PTHR46278:SF4; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR46278; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   Pfam; PF02774; Semialdhyde_dhC; 1.
DR   PIRSF; PIRSF000148; ASA_dh; 1.
DR   SMART; SM00859; Semialdhyde_dh; 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; PS01103; ASD; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009877}.
FT   DOMAIN          11..132
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        145
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT   ACT_SITE        286
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ   SEQUENCE   382 AA;  40870 MW;  2C1504E65745956F CRC64;
     MMTIDHSSAP AVGFVGWRGM VGSVLMDRMR AEGDFADIQP VFFSTSSPGA PAPQIEGLGD
     TGVLQDANDI EALRRLPIIV TAQGGGYTSE VHRKLRETGW DGLWIDAAST LRMEDSSVIA
     LDPVNRDVID AALAGGTKDF VGGNCTVSCM LMGLGGLFRS GLVEWATSMT YQAASGGGAR
     HMREVLRQFG DLSSAVSDEL ADPASAILEI DRRVLDTQRS GQLDVEQFGV PLAGSLIPWI
     DADLGNGQSR EEWKAEKETN KILGLSGDDQ IAIDGLCVRI AAMRSHSQAL TIKLTEDVPV
     EEIERILDAD NEWATVVANE KEASMNGLTP VSASGSLQIP VGRLRKMSMG PQYLSAFTVG
     DQLLWGAAEP LRRMLRIAIG AL
//
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