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Database: UniProt
Entry: A1AYL2_PARDP
LinkDB: A1AYL2_PARDP
Original site: A1AYL2_PARDP 
ID   A1AYL2_PARDP            Unreviewed;       418 AA.
AC   A1AYL2;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Iron-containing alcohol dehydrogenase {ECO:0000313|EMBL:ABL68356.1};
GN   OrderedLocusNames=Pden_0242 {ECO:0000313|EMBL:ABL68356.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68356.1, 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., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|ARBA:ARBA00001962};
CC   -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007358}.
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DR   EMBL; CP000489; ABL68356.1; -; Genomic_DNA.
DR   RefSeq; WP_011746589.1; NC_008686.1.
DR   AlphaFoldDB; A1AYL2; -.
DR   STRING; 318586.Pden_0242; -.
DR   EnsemblBacteria; ABL68356; ABL68356; Pden_0242.
DR   GeneID; 75499794; -.
DR   KEGG; pde:Pden_0242; -.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_0_0_5; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08191; Fe-ADH-like; 1.
DR   Gene3D; 3.40.50.1970; -; 1.
DR   Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR   InterPro; IPR001670; ADH_Fe/GldA.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR11496:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT   DOMAIN          12..390
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   418 AA;  43231 MW;  FEC864BDA6E3546B CRC64;
     MDFTNLGVMR APRHLVFGAG QRGALARHAG VFGTRALIVT DTRMARDKDF LQMRQALEAQ
     GIATQVFDGV AAELPLSCIE AGAKAGRAAG ARMIIGIGGG SCLDAAKIIG LLLSHGGAPQ
     DYYGEYKVPG PIMPLILLPT TSGTGSEVTP VAVLDDPQRA MKIGIASPHL IPEIAICDPE
     LTLSCPPGLT AASGADAMTH AIEAFTTLRR PADSGLSLDH VFIGKNAISD SLALEAIRLI
     AANLARCVSH GDDLEARSAM MLGSTLAGLA FGVAGTAAAH AIQYPVGAMT HTAHGLGVAT
     LMPYVMAWNR PSCETDFARI GAAMGLAASG DTSRQAEAAI AAIAALFAQV GIPATIAQLG
     VPEDRLDEIA RLALSAERLI KNNPRMLDAE GMDRIVRAAH SGDLDLLTAT SPRKAALQ
//
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