ID C1F654_ACIC5 Unreviewed; 353 AA.
AC C1F654;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000313|EMBL:ACO33694.1};
DE EC=1.2.1.11 {ECO:0000313|EMBL:ACO33694.1};
GN Name=asd {ECO:0000313|EMBL:ACO33694.1};
GN OrderedLocusNames=ACP_1463 {ECO:0000313|EMBL:ACO33694.1};
OS Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS 7670 / NBRC 15755 / NCIMB 13165 / 161).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Acidobacterium.
OX NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO33694.1, ECO:0000313|Proteomes:UP000002207};
RN [1] {ECO:0000313|EMBL:ACO33694.1, ECO:0000313|Proteomes:UP000002207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 /
RC NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207};
RX PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT "Three genomes from the phylum Acidobacteria provide insight into the
RT lifestyles of these microorganisms in soils.";
RL Appl. Environ. Microbiol. 75:2046-2056(2009).
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DR EMBL; CP001472; ACO33694.1; -; Genomic_DNA.
DR RefSeq; WP_015896596.1; NC_012483.1.
DR AlphaFoldDB; C1F654; -.
DR STRING; 240015.ACP_1463; -.
DR KEGG; aca:ACP_1463; -.
DR eggNOG; COG0136; Bacteria.
DR HOGENOM; CLU_049966_1_0_0; -.
DR InParanoid; C1F654; -.
DR OrthoDB; 9805684at2; -.
DR Proteomes; UP000002207; 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:ACO33694.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002207}.
FT DOMAIN 4..128
FT /note="Semialdehyde dehydrogenase NAD-binding"
FT /evidence="ECO:0000259|SMART:SM00859"
FT ACT_SITE 147
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
FT ACT_SITE 240
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000148-1"
SQ SEQUENCE 353 AA; 38210 MW; 1804F18B4C720718 CRC64;
MRQKIGILGA TGMVGQRFIQ LLEHHPWFEV AWLAASDRSS GKRYGDAVRW KLDTPIPERI
AAMEISPAQP EGAPQVIFAA LDADIAREME PKFAAAGCAV ISNSSAFRMQ ADVPLVIPEV
NADHLALLEQ QEWRKQSGGY IVTNPNCSAI GLVLALKPLE ERFGIESIFV STMQAVSGAG
YPGVASLDIM GNVVPFIKNE EEKLQEETLR LLGKLQSNLV HPLDAKITAH CNRVAVEDGH
TESVSVKLKR KATREDLLAA WQEFAPLAGR DLPTAPAQPV ETIEAVDRPQ PRLDRMRGAG
MAATVGRVRP CSLLDWKFTV LSHNTIRGAA GAALLNAELL VSLGKLNPSA VPA
//
