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Database: UniProt
Entry: Q12MB1_SHEDO
LinkDB: Q12MB1_SHEDO
Original site: Q12MB1_SHEDO 
ID   Q12MB1_SHEDO            Unreviewed;       356 AA.
AC   Q12MB1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   SubName: Full=Iron-containing alcohol dehydrogenase {ECO:0000313|EMBL:ABE55415.1};
GN   OrderedLocusNames=Sden_2133 {ECO:0000313|EMBL:ABE55415.1};
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161 {ECO:0000313|EMBL:ABE55415.1, ECO:0000313|Proteomes:UP000001982};
RN   [1] {ECO:0000313|EMBL:ABE55415.1, ECO:0000313|Proteomes:UP000001982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS217 / ATCC BAA-1090 / DSM 15013
RC   {ECO:0000313|Proteomes:UP000001982};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:3RF7}
RP   X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH IRON AND NAD.
RG   Joint Center for Structural Genomics (JCSG);
RT   "Crystal structure of an Iron-containing alcohol dehydrogenase (Sden_2133)
RT   from Shewanella denitrificans OS-217 at 2.12 A resolution.";
RL   Submitted (APR-2011) to the PDB data bank.
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DR   EMBL; CP000302; ABE55415.1; -; Genomic_DNA.
DR   RefSeq; WP_011496570.1; NC_007954.1.
DR   PDB; 3RF7; X-ray; 2.12 A; A=1-356.
DR   PDBsum; 3RF7; -.
DR   AlphaFoldDB; Q12MB1; -.
DR   SMR; Q12MB1; -.
DR   STRING; 318161.Sden_2133; -.
DR   DNASU; 4018625; -.
DR   KEGG; sdn:Sden_2133; -.
DR   eggNOG; COG1454; Bacteria.
DR   HOGENOM; CLU_773153_0_0_6; -.
DR   OrthoDB; 9815791at2; -.
DR   Proteomes; UP000001982; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd08184; Fe-ADH_KdnB-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; IPR039697; Alcohol_dehydrogenase_Fe.
DR   PANTHER; PTHR11496:SF104; 3-DEOXY-ALPHA-D-MANNO-OCTULOSONATE 8-OXIDASE; 1.
DR   PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3RF7}; Calcium {ECO:0007829|PDB:3RF7};
KW   Metal-binding {ECO:0007829|PDB:3RF7};
KW   Nucleotide-binding {ECO:0007829|PDB:3RF7};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001982}.
FT   DOMAIN          11..327
FT                   /note="Alcohol dehydrogenase iron-type/glycerol
FT                   dehydrogenase GldA"
FT                   /evidence="ECO:0000259|Pfam:PF00465"
FT   BINDING         42
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         100
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         140
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         149
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         151
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         160
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         191
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         194
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         198
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         258
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0007829|PDB:3RF7"
FT   BINDING         272
FT                   /ligand="Fe(3+)"
FT                   /ligand_id="ChEBI:CHEBI:29034"
FT                   /evidence="ECO:0007829|PDB:3RF7"
SQ   SEQUENCE   356 AA;  39477 MW;  78EB407D9123AD49 CRC64;
     MSFKNFKCVP KMIFGRGSFV QLDTVLEQER TDANDFVVFL VDDVHQHKPL AARVPNKAHD
     LVIYVNVDDE PTTVQVDELT AQVKAFNTKL PVSVVGLGGG STMDLAKAVS LMLTNPGSSS
     EYQGWDLIKN PAVHHIGIPT VSGTGAEASR TAVLCGPVRK LGLNSDYTVF DQIIMDSELI
     AGVPTDQWFY TGMDCFIHCV ESLQGTYLNE FAKAFAEKSM DLCREVYLDD HPEKDDKLMM
     ASYMGGMSIA YSQVGACHAV SYGLGYVLGY HHGIGNCLAF DVLEEFYPEG VAEFRKMMEI
     HNITLPKNIC KDLPDETIAK MVAVTKSMGP LWDNVYGKGW EEKVTDEMLT KLFRRI
//
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