ID   H5WYV9_9PSEU            Unreviewed;       371 AA.
AC   H5WYV9;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Oxidoreductase, Rxyl_3153 family {ECO:0000313|EMBL:EHR51831.1};
GN   ORFNames=SacmaDRAFT_3617 {ECO:0000313|EMBL:EHR51831.1};
OS   Saccharomonospora marina XMU15.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=882083 {ECO:0000313|EMBL:EHR51831.1, ECO:0000313|Proteomes:UP000004926};
RN   [1] {ECO:0000313|EMBL:EHR51831.1, ECO:0000313|Proteomes:UP000004926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=XMU15 {ECO:0000313|EMBL:EHR51831.1,
RC   ECO:0000313|Proteomes:UP000004926};
RX   PubMed=22768369; DOI=10.4056/sigs.2655905;
RA   Klenk H.P., Lu M., Lucas S., Lapidus A., Copeland A., Pitluck S.,
RA   Goodwin L.A., Han C., Tapia R., Brambilla E.M., Potter G., Land M.,
RA   Ivanova N., Rohde M., Goker M., Detter J.C., Li W.J., Kyrpides N.C.,
RA   Woyke T.;
RT   "Genome sequence of the ocean sediment bacterium Saccharomonospora marina
RT   type strain (XMU15(T)).";
RL   Stand. Genomic Sci. 6:265-275(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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DR   EMBL; CM001439; EHR51831.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5WYV9; -.
DR   STRING; 882083.SacmaDRAFT_3617; -.
DR   eggNOG; COG1062; Bacteria.
DR   HOGENOM; CLU_026673_14_1_11; -.
DR   Proteomes; UP000004926; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08279; Zn_ADH_class_III; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR023921; ADH_Zn_actinomycetes.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   NCBIfam; TIGR03989; Rxyl_3153; 1.
DR   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004926};
KW   Zinc {ECO:0000256|RuleBase:RU361277}.
FT   DOMAIN          179..233
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
SQ   SEQUENCE   371 AA;  39392 MW;  4F725D589AA6FC5E CRC64;
     MLMSQTTRAA ICREPGRPWE IAELDLDEPG PNEVRVKFHA AGLCHSDDHI QKGDAQMRFP
     VVGGHEGAGV VDAVGADVTR VAVGDHVVCS FIPACGACRY CSTGRQNLCD EGKNAATGMF
     ADGTFRFHHE GEDLGGLCVL GTFSQYAVVS EWSCITIGQD IPFEIAALVG CGVPTGWGSA
     VYAAGVRAGQ TVVIYGAGGV GSNAVQGARY AGAKNVVVVD PVEFKRDMAA VFGATHTFAD
     AKEAHDFVVE TTWGELADHA IITVGILHDE VIANAIDIVG KSGQVTITAV GNGSVDTHPG
     PLIGYQRRVQ GAIFGGCNPL YDVPRLLGLY RSGDLKLDEL ITRRYRLEEV NQGYEDMLSG
     KNIRGVILHE H
//