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Database: UniProt
Entry: Q2G5I2_NOVAD
LinkDB: Q2G5I2_NOVAD
Original site: Q2G5I2_NOVAD 
ID   Q2G5I2_NOVAD            Unreviewed;       392 AA.
AC   Q2G5I2;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=Iron-containing alcohol dehydrogenase {ECO:0000313|EMBL:ABD26891.1};
GN   OrderedLocusNames=Saro_2455 {ECO:0000313|EMBL:ABD26891.1};
OS   Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS   56034 / CIP 105152 / NBRC 16084 / F199).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=279238 {ECO:0000313|EMBL:ABD26891.1, ECO:0000313|Proteomes:UP000009134};
RN   [1] {ECO:0000313|Proteomes:UP000009134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084
RC   / F199 {ECO:0000313|Proteomes:UP000009134};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA   Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT   "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL   Submitted (JAN-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; CP000248; ABD26891.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2G5I2; -.
DR   STRING; 279238.Saro_2455; -.
DR   DNASU; 3916774; -.
DR   KEGG; nar:Saro_2455; -.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_007207_0_2_5; -.
DR   Proteomes; UP000009134; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08192; MAR-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; PS00060; ADH_IRON_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009134}.
FT   DOMAIN          16..379
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   392 AA;  42006 MW;  C010D789D968D067 CRC64;
     MGSVRASEMT FTETERVTMG RPAREAIRDQ AEKMGARRVF ILASDTLRTK TDEIAAIERE
     LGERHAATFS GIAPHAPRSD VLRAADAARA AGADLIVSVG GGSVTDSAKI VALLLKHDVR
     SVEAFEPLHV YVDGDGNVIN PLAVGPDVRV ICVPTTLSGG EFNALSGATD EAVQHKQGYE
     HRDMAPVMVV LDPALTVYTP EWLWLSTGVR SVDHAVETLA SHLSNDFADG LADSALRLLV
     EGLSRAKADP TDMEARLKCQ IGAWQSMISI IGGVPMGASH AIGHILGGTC DVPHGYTSCV
     MSPYVLAWNA EHDASRQGRI LQCLGNTHAS ASEALDAFIR SLGMPRTLSE VGVGEDRFQQ
     VAEYTMLDIW GRTNPRPVRS PADILEILRK AA
//
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