Y2355_CORGL
ID Y2355_CORGL Reviewed; 304 AA.
AC P0C1E8; P45637;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Uncharacterized protein Cgl2355/cg2587;
DE EC=1.-.-.-;
GN OrderedLocusNames=Cgl2355, cg2587;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; BA000036; BAB99748.1; -; Genomic_DNA.
DR EMBL; BX927155; CAF21020.1; -; Genomic_DNA.
DR RefSeq; NP_601556.1; NC_003450.3.
DR RefSeq; WP_003859319.1; NC_006958.1.
DR AlphaFoldDB; P0C1E8; -.
DR SMR; P0C1E8; -.
DR STRING; 196627.cg2587; -.
DR PRIDE; P0C1E8; -.
DR DNASU; 1020306; -.
DR KEGG; cgb:cg2587; -.
DR KEGG; cgl:Cgl2355; -.
DR PATRIC; fig|196627.13.peg.2291; -.
DR eggNOG; COG0111; Bacteria.
DR HOGENOM; CLU_019796_1_0_11; -.
DR OMA; YGSEEVW; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..304
FT /note="Uncharacterized protein Cgl2355/cg2587"
FT /id="PRO_0000076036"
FT ACT_SITE 217
FT /evidence="ECO:0000250"
FT ACT_SITE 246
FT /evidence="ECO:0000250"
FT ACT_SITE 265
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 136..137
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 215..217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 265..268
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 304 AA; 33053 MW; 80E23C875BCA6DF7 CRC64;
MKFVMYPHLW ESTTAVIEGG GHERVEDIKD ADFIFFNGSA PEFPDLPENI KFVQASMAGI
DALVKRGVVN EKARWANAAG LYADTVAEST IGLILAQMHM HATTRLAKSW SVRPEVENNK
SWLHDNKTVA ILGAGGIGVR LLEMLKPFNV KTIAVNNSGR PVEGADETFA MDKAEHVWAE
ADVFVLILPL TDATYQIVNA ETLGKMKPSA VVVNVGRGPL INTDDLVDAL NNGTIAGAAL
DVTDPEPLPD SHPLWEMDNV VITPHTANTN ERIRALTGEL TLRNIELFEA GEQMATEVDV
VAGY
