CUTB_SULAC
ID CUTB_SULAC Reviewed; 281 AA.
AC Q4J6M6;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Glyceraldehyde dehydrogenase medium chain;
DE EC=1.2.99.8;
DE AltName: Full=Glyceraldehyde dehydrogenase subunit B;
DE AltName: Full=Glyceraldehyde dehydrogenase subunit beta;
GN Name=cutB; OrderedLocusNames=Saci_2269;
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 1-18, 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=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:10095793};
CC Note=Binds 1 FAD per subunit. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000077; AAY81555.1; -; Genomic_DNA.
DR RefSeq; WP_011279057.1; NC_007181.1.
DR AlphaFoldDB; Q4J6M6; -.
DR SMR; Q4J6M6; -.
DR STRING; 330779.Saci_2269; -.
DR EnsemblBacteria; AAY81555; AAY81555; Saci_2269.
DR GeneID; 3474530; -.
DR KEGG; sai:Saci_2269; -.
DR PATRIC; fig|330779.12.peg.2278; -.
DR eggNOG; arCOG01926; Archaea.
DR HOGENOM; CLU_058050_3_0_2; -.
DR OMA; GGTHIYR; -.
DR BioCyc; MetaCyc:MON-17914; -.
DR BRENDA; 1.2.99.8; 6160.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IDA:UniProtKB.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..281
FT /note="Glyceraldehyde dehydrogenase medium chain"
FT /id="PRO_0000424272"
FT DOMAIN 1..176
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 31..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 110..114
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 281 AA; 30863 MW; 9F34004616E96EC6 CRC64;
MYPPEFSYVR AESLQEALKF LEGNDNTRPL AGGQSLIPML KLRVLSPDYI LDINRLNELN
YVKTSLNGVS IGALTRYHDI LSNDIVKSKV PLMHHATRTI GDMQVRNMGT IGGAISNADP
ASDMPVVLTA LNATIILSSA SGSRSVKALD FFKGPFTTDT NKGELVTQIE VPVLDGYKTV
YKKVVRRAGD YALASVALAI KLKGNEIEDI KLAYGGVHDK PFRAMEVEKN VIGKKLNDDL
VKDIASKVSS QINPPSDHRG SSWYRREVVK VLTMKAFKEV A
