ID A0A1U7J7M1_9CYAN Unreviewed; 394 AA.
AC A0A1U7J7M1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:OKH49165.1};
GN ORFNames=NIES30_08380 {ECO:0000313|EMBL:OKH49165.1};
OS Phormidium tenue NIES-30.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=549789 {ECO:0000313|EMBL:OKH49165.1, ECO:0000313|Proteomes:UP000185557};
RN [1] {ECO:0000313|EMBL:OKH49165.1, ECO:0000313|Proteomes:UP000185557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-30 {ECO:0000313|EMBL:OKH49165.1,
RC ECO:0000313|Proteomes:UP000185557};
RA Zhu T., Hou S., Lu X., Hess W.R.;
RT "Draft Genome Sequences of Nine Cyanobacterial Strains from Diverse
RT Habitats.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR000112-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR000112-1};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OKH49165.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MRCG01000004; OKH49165.1; -; Genomic_DNA.
DR RefSeq; WP_073607948.1; NZ_MRCG01000004.1.
DR AlphaFoldDB; A0A1U7J7M1; -.
DR STRING; 549789.NIES30_08380; -.
DR OrthoDB; 5198708at2; -.
DR Proteomes; UP000185557; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR CDD; cd08550; GlyDH-like; 1.
DR Gene3D; 3.40.50.1970; -; 1.
DR Gene3D; 1.20.1090.10; Dehydroquinate synthase-like - alpha domain; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR016205; Glycerol_DH.
DR PANTHER; PTHR43616; GLYCEROL DEHYDROGENASE; 1.
DR PANTHER; PTHR43616:SF3; HYDROXYCARBOXYLATE DEHYDROGENASE A; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000112; Glycerol_dehydrogenase; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000112-1}; NAD {ECO:0000256|PIRSR:PIRSR000112-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000185557};
KW Zinc {ECO:0000256|PIRSR:PIRSR000112-1}.
FT DOMAIN 33..360
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
FT REGION 372..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 105..109
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 136
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 138
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 142
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-3"
FT BINDING 182
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 260
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
FT BINDING 277
FT /ligand="glycerol"
FT /ligand_id="ChEBI:CHEBI:17754"
FT /evidence="ECO:0000256|PIRSR:PIRSR000112-1"
SQ SEQUENCE 394 AA; 40688 MW; E807A9A0FEDEF69C CRC64;
MTTAQLPILA ISPAQVVRGD GILTAQAAMP GGIAAQIARL GQSPLIVGGS HSLKLATPLV
EALGAAGLAT QTVAYGPDCS EAALAHLRSA ATDHQADVVI GMGGGKALDA AKLLAHQLNR
PVVTVPTSGA TCAAWTALSN VYSDQGAFRY DVALATCPNL LILDYALIRT APRRTLVAGI
GDGLAKWYEA AISSGTSQQT LMVAAVQQAR VLRDILLQKT PAALAQWGGP DWQEVVDATV
LLAGVVGGIG GAQCRTVAAH AVHNGLTQLP ASHGILHGEK VAYGILVQLR LEEMGGNAAL
ARAARQQLLP FYQAAGLPQT LADLGLEDMT LSQLQQAAEF ACREGSDIHH LPFTVTPEAV
MAAMVSPLCP ELREKPRDSA SARSSSSVAP EVQP
//