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Database: UniProt
Entry: A0A060NQ50_9BURK
LinkDB: A0A060NQ50_9BURK
Original site: A0A060NQ50_9BURK 
ID   A0A060NQ50_9BURK        Unreviewed;       382 AA.
AC   A0A060NQ50;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Alcohol dehydrogenase, class IV {ECO:0000313|EMBL:BAO83857.1};
GN   Name=yiaY {ECO:0000313|EMBL:BAO83857.1};
GN   ORFNames=SMCB_1629 {ECO:0000313|EMBL:BAO83857.1};
OS   Serpentinimonas maccroryi.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Serpentinimonas.
OX   NCBI_TaxID=1458426 {ECO:0000313|EMBL:BAO83857.1, ECO:0000313|Proteomes:UP000066014};
RN   [1] {ECO:0000313|EMBL:BAO83857.1, ECO:0000313|Proteomes:UP000066014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|EMBL:BAO83857.1,
RC   ECO:0000313|Proteomes:UP000066014};
RX   PubMed=24845058; DOI=10.1038/ncomms4900;
RA   Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA   Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA   Nealson K.H.;
RT   "Physiological and genomic features of highly alkaliphilic hydrogen-
RT   utilizing Betaproteobacteria from a continental serpentinizing site.";
RL   Nat. Commun. 5:3900-3900(2014).
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; AP014569; BAO83857.1; -; Genomic_DNA.
DR   RefSeq; WP_045536171.1; NZ_AP014569.1.
DR   AlphaFoldDB; A0A060NQ50; -.
DR   STRING; 1458426.SMCB_1629; -.
DR   KEGG; cbab:SMCB_1629; -.
DR   HOGENOM; CLU_007207_0_0_4; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000066014; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08188; PDDH; 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.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          11..374
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
SQ   SEQUENCE   382 AA;  39938 MW;  2C0B913435A0916B CRC64;
     MTSTFFMPAV NLMGSGSLGE AMQAVKGLGY RKALIVTDAM LNKLGLADKV AKLLNELQIA
     TVVFDGAQPN PTKGNVRAGL ALLRANQCDC VVSLGGGSSH DCAKGIALCA TNGGEISDYE
     GVDRSVKPQL PLVAINTTAG TASEMTRFCI ITDEETHIKM AIVDRNVTPI LSVNDPDLML
     AKPKALTAAT GMDALTHAVE AYVSTAATPI TDACALKAVE LIARHLRTAV AKGDDLHARE
     QMAYAQFLAG MAFNNASLGY VHAMSHQLGG FYDLPHGVCN ALLLPHVEAF NVKTSAARLR
     DVAQAMGENV QGLDAQAGAQ ACLAAIRKLS SDIGIPKSLG ELGVKRADIP TLAANAMKDA
     CGFTNPRSAT QTEIEAIFEG AM
//
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