ID A0A199PZE9_9MICC Unreviewed; 379 AA.
AC A0A199PZE9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=aspartate-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013120};
DE EC=1.2.1.11 {ECO:0000256|ARBA:ARBA00013120};
GN ORFNames=A5N15_02630 {ECO:0000313|EMBL:OAX66530.1}, AN277_0202235
GN {ECO:0000313|EMBL:OAX52783.1};
OS Rothia kristinae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=37923 {ECO:0000313|EMBL:OAX52783.1, ECO:0000313|Proteomes:UP000053171};
RN [1] {ECO:0000313|EMBL:OAX52783.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RUTW2-3 {ECO:0000313|EMBL:OAX52783.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171};
RA Waterworth S., Matcher G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:OAX52783.1, ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171}, RUTW2-3
RC {ECO:0000313|EMBL:OAX52783.1}, and RUTW4-5
RC {ECO:0000313|EMBL:OAX66530.1, ECO:0000313|Proteomes:UP000092021};
RA Waterworth S.C., Walmsley T.A., Matongo T., Davies-Coleman M.T.,
RA Dorrington R.A.;
RT "Identification of putative biosynthetic pathways for the production of
RT bioactive secondary metabolites by the marine actinomycete Kocuria
RT kristinae RUTW2-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OAX52783.1}.
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DR EMBL; LJBJ02000002; OAX52783.1; -; Genomic_DNA.
DR EMBL; LWGZ01000234; OAX66530.1; -; Genomic_DNA.
DR RefSeq; WP_055684628.1; NZ_LJBJ02000002.1.
DR AlphaFoldDB; A0A199PZE9; -.
DR UniPathway; UPA00034; UER00016.
DR UniPathway; UPA00050; UER00463.
DR UniPathway; UPA00051; UER00464.
DR Proteomes; UP000053171; Unassembled WGS sequence.
DR Proteomes; UP000092021; 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:UP000053171}.
FT DOMAIN 8..129
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 142
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 283
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 379 AA; 41255 MW; 97A5DFCB5E647036 CRC64;
MTFHPGDPVG FVGWRGMVGS VLMQRLEQEG DFADFTPVFF STSAAGSPAP TFRGAEEPST
LQDAHDLDEL ALLPVIVTTQ GGDYTKAVHG KLRERGWDGL WIDAASTLRQ EPDSVIVLDP
VNRDVIDRAL EAGIRDFIGG NCTVSCLLMG LGGLFRRGLV QWSTAMTYQA ASGGGARHMR
EVLAGFRDVA GTVAQELSDP ASAILEVDRK VLAMQRSGEL DTTQFEVPLA GSLIPWIDAD
LGNRQSREEW KADAETNKIL GLDGDDRVVM DGLCVRIATM RSHAQALTMK LTEDLSVEEI
ERIIDEDNEW AHVVPNTKED TIRDLTPVAA SGSLRIPVGR VRKLAMGPEY ISAFTVGDQL
LWGAAEPVRR MLKIAVGTR
//
