CUTC_SULAC
ID CUTC_SULAC Reviewed; 163 AA.
AC Q4J6M5;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Glyceraldehyde dehydrogenase small chain;
DE EC=1.2.99.8;
DE AltName: Full=Glyceraldehyde dehydrogenase subunit C;
DE AltName: Full=Glyceraldehyde dehydrogenase subunit gamma;
GN Name=cutC; OrderedLocusNames=Saci_2270;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP PROTEIN SEQUENCE OF 1-21, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RX PubMed=10095793; DOI=10.1046/j.1432-1327.1999.00201.x;
RA Kardinahl S., Schmidt C.L., Hansen T., Anemuller S., Petersen A.,
RA Schafer G.;
RT "The strict molybdate-dependence of glucose-degradation by the
RT thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic
RT molybdenum containing enzyme--an aldehyde oxidoreductase.";
RL Eur. J. Biochem. 260:540-548(1999).
CC -!- FUNCTION: Component of the glyceraldehyde dehydrogenase which is
CC involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the
CC oxidation of D-glyceraldehyde to yield glycerate. When the artificial
CC electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the
CC enzyme shows a broad substrate range (glyceraldehyde-3-phosphate,
CC formaldehyde, acetaldehyde, propionaldehyde and isobutyraldehyde), but
CC is most active with D-glyceraldehyde. It is not known which acceptor is
CC utilized in vivo. {ECO:0000269|PubMed:10095793}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + D-glyceraldehyde + H2O = (R)-glycerate + AH2 + H(+);
CC Xref=Rhea:RHEA:36047, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16659, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:17499; EC=1.2.99.8;
CC Evidence={ECO:0000269|PubMed:10095793};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:10095793};
CC Note=Binds 2 [2Fe-2S] cluster per subunit.
CC {ECO:0000269|PubMed:10095793};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for propionaldehyde (at 80 degrees Celsius and pH 6.7)
CC {ECO:0000269|PubMed:10095793};
CC KM=90 uM for D,L-glyceraldehyde (at 80 degrees Celsius and pH 6.7)
CC {ECO:0000269|PubMed:10095793};
CC pH dependence:
CC Optimum pH is 6.7. At pH 6.7, glyceraldehyde is the predominant
CC substrate, however at pH 7.5 the dehydrogenase exhibits activity
CC preferentially towards the aliphatic aldehydes such as formaldehyde,
CC acetaldehyde and propionaldehyde. {ECO:0000269|PubMed:10095793};
CC -!- SUBUNIT: Heterotrimer composed of a large chain (CutA), a medium chain
CC (CutB) and a small chain (CutC). {ECO:0000269|PubMed:10095793}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10095793}.
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DR EMBL; CP000077; AAY81556.1; -; Genomic_DNA.
DR RefSeq; WP_011279058.1; NC_007181.1.
DR AlphaFoldDB; Q4J6M5; -.
DR SMR; Q4J6M5; -.
DR STRING; 330779.Saci_2270; -.
DR EnsemblBacteria; AAY81556; AAY81556; Saci_2270.
DR GeneID; 3474531; -.
DR KEGG; sai:Saci_2270; -.
DR PATRIC; fig|330779.12.peg.2279; -.
DR eggNOG; arCOG01925; Archaea.
DR HOGENOM; CLU_052511_3_1_2; -.
DR OMA; EHDVPQC; -.
DR BioCyc; MetaCyc:MON-17915; -.
DR BRENDA; 1.2.99.8; 6160.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IDA:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR Pfam; PF00111; Fer2; 1.
DR Pfam; PF01799; Fer2_2; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Cytoplasm; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..163
FT /note="Glyceraldehyde dehydrogenase small chain"
FT /id="PRO_0000424273"
FT DOMAIN 10..86
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 48
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 163 AA; 17856 MW; B81B889CA7553E2A CRC64;
MLVVKKGEGV KVRVRVNGVW YEKYVSPRTL LVDFIRDELG LTGTKVGCDT TTCGACTVIM
NGKSVKSCTV LAAQADGAEI TTIEGLSSDS KLHPIQEAFK DNFALQCGFC TAGMIMQTYF
FLKEHPNPTE EEVRDGIHGN ICRCTGYQNI VKAVLDASKR LRS
