ID B0VJ11_CLOAI Unreviewed; 352 AA.
AC B0VJ11;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=3,5-diaminohexanoate dehydrogenase {ECO:0000313|EMBL:CAO81203.1};
DE EC=1.4.1.11 {ECO:0000313|EMBL:CAO81203.1};
GN Name=kdd {ECO:0000313|EMBL:CAO81203.1};
GN OrderedLocusNames=CLOAM1348 {ECO:0000313|EMBL:CAO81203.1};
OS Cloacimonas acidaminovorans (strain Evry).
OC Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO81203.1, ECO:0000313|Proteomes:UP000002019};
RN [1] {ECO:0000313|EMBL:CAO81203.1, ECO:0000313|Proteomes:UP000002019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX PubMed=18245282; DOI=10.1128/JB.01248-07;
RA Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA Weissenbach J., Le Paslier D.;
RT "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT provides a first glimpse of a new bacterial division.";
RL J. Bacteriol. 190:2572-2579(2008).
RN [2] {ECO:0007829|PDB:7DL0, ECO:0007829|PDB:7DL1}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH NADP(+).
RX PubMed=33624917; DOI=10.1002/anie.202017225;
RA Liu N., Wu L., Feng J., Sheng X., Li J., Chen X., Li J., Liu W., Zhou J.,
RA Wu Q., Zhu D.;
RT "Crystal Structures and Catalytic Mechanism of l-erythro-3,5-
RT Diaminohexanoate Dehydrogenase and Rational Engineering for Asymmetric
RT Synthesis of beta-Amino Acids.";
RL Angew. Chem. Int. Ed. 60:10203-10210(2021).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; CU466930; CAO81203.1; -; Genomic_DNA.
DR RefSeq; WP_015425061.1; NC_020449.1.
DR PDB; 7DL0; X-ray; 2.17 A; A/B=1-352.
DR PDB; 7DL1; X-ray; 2.72 A; A/B/C/D=1-352.
DR PDB; 7DL3; X-ray; 1.85 A; A/B/C/D=1-352.
DR PDB; 7DL7; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-352.
DR AlphaFoldDB; B0VJ11; -.
DR SMR; B0VJ11; -.
DR STRING; 459349.CLOAM1348; -.
DR KEGG; caci:CLOAM1348; -.
DR eggNOG; COG0604; Bacteria.
DR HOGENOM; CLU_826176_0_0_0; -.
DR OrthoDB; 48703at2; -.
DR Proteomes; UP000002019; Chromosome.
DR GO; GO:0047124; F:L-erythro-3,5-diaminohexanoate dehydrogenase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43350; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR43350:SF17; NAD-DEPENDENT ALCOHOL DEHYDROGENASE; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7DL0, ECO:0007829|PDB:7DL1};
KW Nucleotide-binding {ECO:0007829|PDB:7DL0, ECO:0007829|PDB:7DL1};
KW Oxidoreductase {ECO:0000313|EMBL:CAO81203.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002019}.
FT DOMAIN 205..298
FT /note="Alcohol dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00107"
FT BINDING 49
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 51
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL1, ECO:0007829|PDB:7DL3"
FT BINDING 203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 204
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 204
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL1, ECO:0007829|PDB:7DL3"
FT BINDING 227
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL1, ECO:0007829|PDB:7DL3"
FT BINDING 227
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL1, ECO:0007829|PDB:7DL3"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL1, ECO:0007829|PDB:7DL3"
FT BINDING 248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 274
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL1"
FT BINDING 274
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 275
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL1"
FT BINDING 276
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL1, ECO:0007829|PDB:7DL3"
FT BINDING 276
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 296
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 298
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL1, ECO:0007829|PDB:7DL3"
FT BINDING 298
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
FT BINDING 310
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7DL3"
FT BINDING 321
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7DL0"
SQ SEQUENCE 352 AA; 38279 MW; 47AA271C6D825D19 CRC64;
MKSNGCRYGT HRVIEPKGVL PQPAKILNND MSEIWDNEML IDVIRLNIDS ASFHQIKNKL
IAQGHQDLEK AFAEHAIELT NRTGKHKNED TGSGGMFIGR VAAIGDKFEM KEEVKVGDKI
ASLVSLSLTP LKINKVKKVL LDKDQMEIEG QAILFSSGVY AKLPDDLDEN LALSVLDVAG
APAQVERLVK PDDTVVIIGA NGKSGILCNA VAKERAGICG KVIGVVRNEN YIPTCKATGC
DEVILAQATD AITIQKEVSR LTNGKMADVV INVVNTEDTE LPSIMAAKDR GMVYFFSMAT
SFTKAALGAE GIGADVDMMI GNGYAHHHSE IALDLLRRNS VLMKIFKERY AE
//
