SUCD_METS5
ID SUCD_METS5 Reviewed; 360 AA.
AC A4YGN0;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Succinate-semialdehyde dehydrogenase (acetylating);
DE EC=1.2.1.76;
GN OrderedLocusNames=Msed_1424;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(2008).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18079405; DOI=10.1126/science.1149976;
RA Berg I.A., Kockelkorn D., Buckel W., Fuchs G.;
RT "A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide
RT assimilation pathway in Archaea.";
RL Science 318:1782-1786(2007).
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. Participates in the 3-
CC hydroxypropanoate/4-hydroxybutyrate cycle, an autotrophic CO(2)
CC fixation pathway found in some thermoacidophilic archaea.
CC {ECO:0000269|PubMed:18079405}.
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 Evidence={ECO:0000269|PubMed:18079405};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; CP000682; ABP95582.1; -; Genomic_DNA.
DR RefSeq; WP_012021369.1; NC_009440.1.
DR AlphaFoldDB; A4YGN0; -.
DR SMR; A4YGN0; -.
DR STRING; 399549.Msed_1424; -.
DR PRIDE; A4YGN0; -.
DR EnsemblBacteria; ABP95582; ABP95582; Msed_1424.
DR GeneID; 5104795; -.
DR GeneID; 59457468; -.
DR KEGG; mse:Msed_1424; -.
DR eggNOG; arCOG01456; Archaea.
DR HOGENOM; CLU_026673_14_1_2; -.
DR OMA; IHHYMGT; -.
DR BioCyc; MetaCyc:MON-13734; -.
DR BRENDA; 1.1.1.B47; 7245.
DR Proteomes; UP000000242; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 2.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Metal-binding; NADP; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..360
FT /note="Succinate-semialdehyde dehydrogenase (acetylating)"
FT /id="PRO_0000413681"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 189..194
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 279..281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 37879 MW; 4032D0DE537025D9 CRC64;
MKAAVLHTYK EPLSIEDVNI SQPKAGEVKI KVKATGLCHS DVNVFEGKTP VPPPVVAGHE
ISGIVEEVGP GVTRVKPGDR VISAFIHPCG KCGNCVAGKE NLCETFSQVR LKGVMPDGTS
RLSKDGKEIR TFLGGGFAEY AIVGENALTR VPEDMDLEKV AVLGCAGLTG YGAISSSKIE
PGDTVAVIGV GGVGLSTIQL LRASGAGRII AVGTKKWKLD RAMELGATDV VNSKEIDPVK
AIKEITGGGP QVVIEAGGNE DTIHMALDSV RIGGKVVLVG LPPATAMIPI RVASIVRGGI
EVVGNYGGRP RVDMPKLLEL VRQGRYDPSR LVTGRFRLEE INEAVKMLEE GEAIRSLIIP
