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Database: UniProt
Entry: R5QPM2_9PROT
LinkDB: R5QPM2_9PROT
Original site: R5QPM2_9PROT 
ID   R5QPM2_9PROT            Unreviewed;       336 AA.
AC   R5QPM2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Aspartate-semialdehyde dehydrogenase 2 {ECO:0000313|EMBL:CCZ30665.1};
GN   ORFNames=BN682_00592 {ECO:0000313|EMBL:CCZ30665.1};
OS   Proteobacteria bacterium CAG:495.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=1262987 {ECO:0000313|EMBL:CCZ30665.1, ECO:0000313|Proteomes:UP000018309};
RN   [1] {ECO:0000313|EMBL:CCZ30665.1, ECO:0000313|Proteomes:UP000018309}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:495 {ECO:0000313|Proteomes:UP000018309};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCZ30665.1}.
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DR   EMBL; CAZU010000068; CCZ30665.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5QPM2; -.
DR   STRING; 1262987.BN682_00592; -.
DR   Proteomes; UP000018309; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR   PANTHER; PTHR46278:SF2; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018309}.
FT   DOMAIN          3..119
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
SQ   SEQUENCE   336 AA;  36650 MW;  119183416753E081 CRC64;
     MKKIAVVGVQ ESIGREILSY LAEEGYKPEQ VVALEPKSAL GNMVSFGEDD ELDVESLDKF
     DFSGVAAAVF CVAAEVAKKY VPHALAKGVK VVDCSSAFFG DPDVPMIISG INGEKLSAAK
     RGLVMVPSAG VTQMLLPLKN IHEQYQITRI VVSDYTSTSV YGKEGMDELF NQTRKIFMND
     TLVDDQQVFH KQVAFNVIPQ VGDFQGDETV VEWAFNAETK QILGPDVRVH ANCAIIPAFI
     GCGQYVNVEC AKDIDVEDAR ELMKKVPGIV VFDKHIDGGY VTVNDVQGEN DIYISRLRQD
     TSVENGISFW CVADNLRAGV AKNALAVAKL LTETSD
//
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