ID A0A0A7I0H1_9BIFI Unreviewed; 364 AA.
AC A0A0A7I0H1;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:AIZ13797.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:AIZ13797.1};
GN ORFNames=AH68_00815 {ECO:0000313|EMBL:AIZ13797.1};
OS Bifidobacterium catenulatum PV20-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ13797.1, ECO:0000313|Proteomes:UP000030625};
RN [1] {ECO:0000313|EMBL:AIZ13797.1, ECO:0000313|Proteomes:UP000030625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ13797.1,
RC ECO:0000313|Proteomes:UP000030625};
RX PubMed=25614572;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C.,
RA Stevens M.J.;
RT "Complete and Assembled Genome Sequence of Bifidobacterium kashiwanohense
RT PV20-2, Isolated from the Feces of an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP007456; AIZ13797.1; -; Genomic_DNA.
DR RefSeq; WP_039196754.1; NZ_CP007456.1.
DR AlphaFoldDB; A0A0A7I0H1; -.
DR STRING; 1447716.AH68_00815; -.
DR KEGG; bka:AH68_00815; -.
DR HOGENOM; CLU_049966_1_0_11; -.
DR OrthoDB; 9805684at2; -.
DR Proteomes; UP000030625; Chromosome.
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:0008652; P:amino acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005676; Asp_semi-ald_DH_pep-lack.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom.
DR NCBIfam; TIGR00978; asd_EA; 1.
DR PANTHER; PTHR46718; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR46718:SF1; ASPARTATE-SEMIALDEHYDE DEHYDROGENASE; 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 4: Predicted;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:AIZ13797.1}.
FT DOMAIN 6..138
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 158
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 254
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 364 AA; 40469 MW; 8218FE71A8E395FC CRC64;
MSEKIKVGIL GATGMVGQRF VTLLENHPWF ELVTLAASAH SAGKTYEEAI GGRWKMETPM
PEFVKNMVVK NVADVEDVVK NVDFVFSAVN MPKAEIRAIE EEYAKTETPV VSNNSAHRWT
PDVPMVVPEI NPEHYEVIEH QRKRLGTTHG FIAVKPNCSI QAYTPALAAW KEFEPREVIV
STYQAISGAG KTFNDWPEML GNIIPFISGE EEKSEKEPLK VFGHVDEEKG EIVPFDGPLK
ITSQCIRVPV LNGHTATVFI NFGKNPTKEE LVDRLVNYTS QASELGLPHA PKQFIQYLTD
DDRPQVKKDV DYEGGMGVSI GRLREDSIFD WKFVGLAHNT LRGAAGGALE SAEMLKALGY
ITKK
//
