(data stored in SCRATCH zone)

SWISSPROT: A1AXY9_PARDP

ID   A1AXY9_PARDP            Unreviewed;       375 AA.
AC   A1AXY9;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   RecName: Full=S-(hydroxymethyl)glutathione dehydrogenase {ECO:0000256|RuleBase:RU362016};
DE            EC=1.1.1.284 {ECO:0000256|RuleBase:RU362016};
GN   OrderedLocusNames=Pden_0016 {ECO:0000313|EMBL:ABL68133.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68133.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-
CC         formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58758; EC=1.1.1.284;
CC         Evidence={ECO:0000256|RuleBase:RU362016};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU362016};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily. {ECO:0000256|RuleBase:RU362016}.
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DR   EMBL; CP000489; ABL68133.1; -; Genomic_DNA.
DR   RefSeq; WP_011746366.1; NC_008686.1.
DR   STRING; 318586.Pden_0016; -.
DR   PRIDE; A1AXY9; -.
DR   EnsemblBacteria; ABL68133; ABL68133; Pden_0016.
DR   KEGG; pde:Pden_0016; -.
DR   eggNOG; ENOG4107QPD; Bacteria.
DR   eggNOG; COG1062; LUCA.
DR   HOGENOM; HOG000294674; -.
DR   KO; K00121; -.
DR   OMA; ATHKGWG; -.
DR   BioCyc; PDEN318586:G1GW1-16-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006069; P:ethanol oxidation; IEA:InterPro.
DR   CDD; cd08300; alcohol_DH_class_III; 1.
DR   InterPro; IPR014183; ADH_3.
DR   InterPro; IPR013149; ADH_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   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; SSF50129; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR02818; adh_III_F_hyde; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AXY9.
DR   SWISS-2DPAGE; A1AXY9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Metal-binding {ECO:0000256|RuleBase:RU362016};
KW   NAD {ECO:0000256|RuleBase:RU362016};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362016};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Zinc {ECO:0000256|RuleBase:RU362016}.
FT   DOMAIN       28    121       ADH_N. {ECO:0000259|Pfam:PF08240}.
FT   DOMAIN      198    337       ADH_zinc_N. {ECO:0000259|Pfam:PF00107}.
SQ   SEQUENCE   375 AA;  39920 MW;  ABAB86BDF891D1A9 CRC64;
     MRTRAAVALE AGKPLEVMEV NLEGPKAGEV MVEIKATGIC HTDEFTLSGA DPEGLFPSIL
     GHEGAGVVVE VGPGVTSVKP GDHVIPLYTP ECRQCASCLS GKTNLCTAIR ATQGQGLMPD
     GTSRFSMLDG TPIFHYMGCS TFSNYTVLPE IAVAKVREDA PFDKICYIGC GVTTGIGAVI
     NTAKVEIGAK AVVFGLGGIG LNVLQGLRLA GADMIIGVDL NDDKKPMAEH FGMTHFINPK
     NCENVVQEIV NLTKTPFDQI GGADYSFDCT GNVKVMRDAL ECTHRGWGQS IIIGVAPAGA
     EISTRPFQLV TGRVWKGTAF GGARGRTDVP QIVDWYMDGK IEIDPMITHT LSLDDINKGF
     DLMHAGESIR SVVLY
//

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