ID A0A0A7I596_9BIFI Unreviewed; 334 AA.
AC A0A0A7I596;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:AIZ13964.1};
GN ORFNames=AH68_01750 {ECO:0000313|EMBL:AIZ13964.1};
OS Bifidobacterium catenulatum PV20-2.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1447716 {ECO:0000313|EMBL:AIZ13964.1, ECO:0000313|Proteomes:UP000030625};
RN [1] {ECO:0000313|EMBL:AIZ13964.1, ECO:0000313|Proteomes:UP000030625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV20-2 {ECO:0000313|EMBL:AIZ13964.1,
RC ECO:0000313|Proteomes:UP000030625};
RX PubMed=25614572;
RA Vazquez-Gutierrez P., Lacroix C., Chassard C., Klumpp J., Jans C.,
RA Stevens M.J.;
RT "Complete and Assembled Genome Sequence of Bifidobacterium kashiwanohense
RT PV20-2, Isolated from the Feces of an Anemic Kenyan Infant.";
RL Genome Announc. 3:0-0(2015).
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; CP007456; AIZ13964.1; -; Genomic_DNA.
DR RefSeq; WP_039197056.1; NZ_CP007456.1.
DR AlphaFoldDB; A0A0A7I596; -.
DR STRING; 1447716.AH68_01750; -.
DR KEGG; bka:AH68_01750; -.
DR HOGENOM; CLU_026673_11_0_11; -.
DR OrthoDB; 3987021at2; -.
DR Proteomes; UP000030625; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd08234; threonine_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 InterPro; IPR020843; PKS_ER.
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 SMART; SM00829; PKS_ER; 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 8..330
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 334 AA; 35751 MW; 7B05D14D7600791B CRC64;
MKALVLTGVK KLEIQNMPTP QIEPDEVLIN TAYAGVCGTD HDLYDGRPGS AAAVPPIVLG
HENSGIVAAV GADVTNVKPG DRVAVDPNIY CGQCEFCLTQ RPELCDHLSA VGVTRNGGLA
EQFTAPASVV YKLPDNVSLR DAAAVEPVSC AVHGLDLLEL RPYQKALVIG DGFMGQIFAQ
LLQAYGVHQV DLAGIFDEKL QRNKEQFGVT ETYNTTREQI PEDSYDVIIE AVGLPATQAQ
AVAAAKKGAQ VLMFGVGPQE AHFEMNTYDI YKKQLTIQGS FINPLTFRDA ISLVSSGKMN
IGGLISHELE LEQVQDFLDG KITGVSKAVV KIGA
//
