CUTA_SULAC
ID CUTA_SULAC Reviewed; 748 AA.
AC Q4J6M3;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Glyceraldehyde dehydrogenase large chain;
DE EC=1.2.99.8;
DE AltName: Full=Glyceraldehyde dehydrogenase subunit A;
DE AltName: Full=Glyceraldehyde dehydrogenase subunit alpha;
GN Name=cutA; OrderedLocusNames=Saci_2271;
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 2-21, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, 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=Mo-molybdopterin guanine dinucleotide; Xref=ChEBI:CHEBI:71310;
CC Evidence={ECO:0000269|PubMed:10095793};
CC Note=Binds 1 Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor
CC 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 -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; CP000077; AAY81557.1; -; Genomic_DNA.
DR RefSeq; WP_011279059.1; NC_007181.1.
DR AlphaFoldDB; Q4J6M3; -.
DR SMR; Q4J6M3; -.
DR STRING; 330779.Saci_2271; -.
DR EnsemblBacteria; AAY81557; AAY81557; Saci_2271.
DR GeneID; 3474532; -.
DR KEGG; sai:Saci_2271; -.
DR PATRIC; fig|330779.12.peg.2280; -.
DR eggNOG; arCOG01167; Archaea.
DR HOGENOM; CLU_001681_2_0_2; -.
DR OMA; THYYQTV; -.
DR BioCyc; MetaCyc:MON-17913; -.
DR BRENDA; 1.2.99.8; 6160.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043795; F:glyceraldehyde oxidoreductase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
DR GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IDA:UniProtKB.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR PANTHER; PTHR11908; PTHR11908; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Metal-binding; Molybdenum;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10095793"
FT CHAIN 2..748
FT /note="Glyceraldehyde dehydrogenase large chain"
FT /id="PRO_0000424271"
FT BINDING 247
FT /ligand="Mo-molybdopterin guanine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71310"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="Mo-molybdopterin guanine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71310"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="Mo-molybdopterin guanine dinucleotide"
FT /ligand_id="ChEBI:CHEBI:71310"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
SQ SEQUENCE 748 AA; 82572 MW; 4CB3F410FD308DB2 CRC64;
MTYTGKSIKR LNDDKFITGR SNYIDDIKIP SLYAGFVRSP YPHAIIKRID ATDALKVNGI
VAVFSGKDIN PMLKGGVGVL SAYVNPSLFR FKERKAFPED NKVKYVGEPV AIVIGQDKYA
VRDAIDRVNV EYEQLKPVIK MEDAEKDEVI VHDELKTNVS YKIPFKAGDI EKAFSQADKV
VKVEAINERL IPNPMEPRGI LSVYDGNSLS VWYSTQVPHF ARSEFARIFG IPETKIRVAM
PDVGGAFGSK VHIMAEELAV IASSILLRRP VRWTATRSEE MLASEARSNV FTGEVAVKKD
GTVLGIKGKL LLDLGAYLTL TAGIQPTIIP VMIPGPYKVR DLEIESTAVY TTTPPITMYR
GASRPEATYI IERIMSTVAD ELGLDDVTIR ERNLIDQLPY TNPFGLRYDT GDYIRVFKDG
VAKLEYNELR KWAQQERSKG HRVGVGLAFY LEICSFGPWE YGEIKVDNKG NVLVITGTTP
HGQGTETAIA QIVADALQIP IEKIRVVWGD TDIVEGSFGT YGSRSLTIGG SAALKVAERV
LDKMKRAAAS YFNADVQEIR YENEEFSVKN DPSKKASWDE IASLATTKEP IVEKIYYEND
VTFPYGVHVA VVEVDDLGMA RVVEYRAYDD IGKVINPALA EAQIHGGGVQ GVGQALYEKA
IINENGQLSV TYADYYVPTA VEAPRFISYF ADKSHPSNYP TGTKGVGEAA LIVGPAAIIR
AIEDAVGARF TKTPTPPEEI YKAIMSKK
