ID   SUCD_CLOK5              Reviewed;         453 AA.
AC   P38947; A5N1M7;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase (acetylating);
DE            EC=1.2.1.76;
GN   Name=sucD; OrderedLocusNames=CKL_3015;
OS   Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=431943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-24.
RX   PubMed=8550525; DOI=10.1128/jb.178.3.871-880.1996;
RA   Soehling B., Gottschalk G.;
RT   "Molecular analysis of the anaerobic succinate degradation pathway in
RT   Clostridium kluyveri.";
RL   J. Bacteriol. 178:871-880(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8527 / DSM 555 / NCIMB 10680;
RX   PubMed=18218779; DOI=10.1073/pnas.0711093105;
RA   Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H.,
RA   Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F.,
RA   Hagemeier C., Thauer R.K., Gottschalk G.;
RT   "The genome of Clostridium kluyveri, a strict anaerobe with unique
RT   metabolic features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008).
CC   -!- FUNCTION: Catalyzes the reduction of succinate semialdehyde to
CC       succinyl-CoA. The enzyme is specific for succinate semialdehyde and
CC       succinyl-CoA, and only shows low activity with palmitoyl-CoA. There is
CC       no activity with NAD(+) as cosubstrate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CoA + NADP(+) + succinate semialdehyde = H(+) + NADPH +
CC         succinyl-CoA; Xref=Rhea:RHEA:26450, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57706,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.2.1.76;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.3 mM for NADPH;
CC         KM=3.2 mM for succinyl-CoA;
CC         KM=2.7 mM for succinate semialdehyde;
CC         KM=2.9 mM for CoA;
CC         KM=4.0 mM for NADP(+);
CC         Vmax=28.9 umol/min/mg enzyme toward NADPH;
CC         Vmax=28.9 umol/min/mg enzyme toward succinyl-CoA;
CC         Vmax=28.3 umol/min/mg enzyme toward succinate semialdehyde;
CC         Vmax=27.3 umol/min/mg enzyme toward CoA;
CC         Vmax=31.2 umol/min/mg enzyme toward NADP(+);
CC       pH dependence:
CC         Optimum pH is 7.0 for the reduction reaction and 8.5 for the
CC         oxidation reaction.;
CC   -!- SUBUNIT: Homodimer.
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DR   EMBL; L21902; AAA92347.1; -; Genomic_DNA.
DR   EMBL; CP000673; EDK35023.1; -; Genomic_DNA.
DR   RefSeq; WP_012103358.1; NC_009706.1.
DR   AlphaFoldDB; P38947; -.
DR   SMR; P38947; -.
DR   STRING; 431943.CKL_3015; -.
DR   EnsemblBacteria; EDK35023; EDK35023; CKL_3015.
DR   KEGG; ag:AAA92347; -.
DR   KEGG; ckl:CKL_3015; -.
DR   eggNOG; COG1012; Bacteria.
DR   HOGENOM; CLU_028794_3_1_9; -.
DR   OMA; INQIQCF; -.
DR   OrthoDB; 384611at2; -.
DR   BioCyc; MetaCyc:MON-13462; -.
DR   Proteomes; UP000002411; Chromosome.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..453
FT                   /note="Succinate-semialdehyde dehydrogenase (acetylating)"
FT                   /id="PRO_0000072297"
FT   ACT_SITE        242
FT                   /evidence="ECO:0000250"
FT   BINDING         188..193
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        16
FT                   /note="V -> A (in Ref. 1; AAA92347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        379
FT                   /note="A -> ARTVLPISRLVVNQPATTAG (in Ref. 1; AAA92347)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   453 AA;  48968 MW;  61706F0AEBC865D7 CRC64;
     MSNEVSIKEL IEKAKVAQKK LEAYSQEQVD VLVKALGKVV YDNAEMFAKE AVEETEMGVY
     EDKVAKCHLK SGAIWNHIKD KKTVGIIKEE PERALVYVAK PKGVVAATTP ITNPVVTPMC
     NAMAAIKGRN TIIVAPHPKA KKVSAHTVEL MNAELKKLGA PENIIQIVEA PSREAAKELM
     ESADVVIATG GAGRVKAAYS SGRPAYGVGP GNSQVIVDKG YDYNKAAQDI ITGRKYDNGI
     ICSSEQSVIA PAEDYDKVIA AFVENGAFYV EDEETVEKFR STLFKDGKIN SKIIGKSVQI
     IADLAGVKVP EGTKVIVLKG KGAGEKDVLC KEKMCPVLVA LKYDTFEEAV EIAMANYMYE
     GAGHTAGIHS DNDENIRYAG TVLPISRLVV NQPATTAGGS FNNGFNPTTT LGCGSWGRNS
     ISENLTYEHL INVSRIGYFN KEAKVPSYEE IWG