ID A0A1G6ZCA3_9SPHI Unreviewed; 401 AA.
AC A0A1G6ZCA3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:SDE00258.1};
GN ORFNames=SAMN05216464_103298 {ECO:0000313|EMBL:SDE00258.1};
OS Mucilaginibacter pineti.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDE00258.1, ECO:0000313|Proteomes:UP000199072};
RN [1] {ECO:0000313|EMBL:SDE00258.1, ECO:0000313|Proteomes:UP000199072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47C3B {ECO:0000313|EMBL:SDE00258.1,
RC ECO:0000313|Proteomes:UP000199072};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC 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; FNAI01000003; SDE00258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6ZCA3; -.
DR STRING; 1391627.SAMN05216464_103298; -.
DR OrthoDB; 9787435at2; -.
DR Proteomes; UP000199072; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08283; FDH_like_1; 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; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42813:SF2; DEHYDROGENASE, ZINC-CONTAINING, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G02810)-RELATED; 1.
DR PANTHER; PTHR42813; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000199072};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 26..149
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 196..327
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 401 AA; 44233 MW; 5DC01D799DCE44E3 CRC64;
MKAAVFHKPG DIRYDTVEDP RIEQDTDVIL RVTSTAICGS DLHILSGGVP QPKPMVMGHE
FMGIVEEVGK GVTQLKKGDR VVVPFPISCG HCFFCQHDAS PACEHSNYKH YGPNGDMLDQ
KGAALFGYTD LYGGYSGGQA EYVRVPYADI SPRVVPENMS DEQVLFLTDI FPTGWSAIDW
AQLKGGEVVA IFGSGPVGLM AQKAAWINGA SRVIAIDPLN YRLEKAKAVN KVETLNPHEV
DVVEAIRAMT GGRGADVCVD AVGFEPERDL LDKAKALFNF EVGSMKVLDM AFKAVRRMGT
VSIMGVYGST YDNFPLHRVF DKGITLKMGQ APVLNYIDHL IDLVKTEKVV LDDIITHTLP
LSEVTHGYEI FDKKEEDCVK VVLKPWEQRK ETNEEPVKID N
//