ID U5RXL3_9CLOT Unreviewed; 364 AA.
AC U5RXL3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Zinc-dependent dehydrogenase {ECO:0000313|EMBL:AGY77450.1};
GN ORFNames=CAETHG_3247 {ECO:0000313|EMBL:AGY77450.1};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY77450.1, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY77450.1, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY77450.1};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
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; CP006763; AGY77450.1; -; Genomic_DNA.
DR RefSeq; WP_013237821.1; NZ_CP012395.1.
DR AlphaFoldDB; U5RXL3; -.
DR KEGG; cah:CAETHG_3247; -.
DR PATRIC; fig|1341692.11.peg.3259; -.
DR HOGENOM; CLU_026673_11_0_9; -.
DR Proteomes; UP000017590; Chromosome.
DR GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd08235; iditol_2_DH_like; 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; PTHR43401; L-THREONINE 3-DEHYDROGENASE; 1.
DR PANTHER; PTHR43401:SF2; L-THREONINE 3-DEHYDROGENASE; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 25..127
FT /note="Alcohol dehydrogenase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08240"
FT DOMAIN 176..299
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
SQ SEQUENCE 364 AA; 39048 MW; CDB31CC642B59A5B CRC64;
MKAAIYKGIG KIELEEIAKP KVEKGTVLIK VKACAICGGD LRTFNFGHKS IKPPIVLGHE
IAGEIVETAS DIEKYKVGDR VIVAPAIGCG SCSYCLSGWQ NMCYHRTTIA HHYNGGFEEY
MLIPAAAIKA GNINYIPDEV TYLEASLAEP LACVLNAQEV INVGLGDTVA VIGAGPIGCM
HAEVARAKGA GKVFLINRSE GRLQATKKFG FDEYICSGKE DAVKAVMDLT NGLGANIVIV
TAGSPEAEIM GLNMASKMGK VCFFAGLPKD QPTVNLDSNL LHYRQITVFG TFSSAPRHNA
LALEMIRSGK VSAKDILTHV VTLDKIIDGM KLVKNREALR VSVAPCIDEI NDEFNKLPGV
KIVK
//
