ID A0A2B8B7H3_9PROT Unreviewed; 388 AA.
AC A0A2B8B7H3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:PGH57234.1};
GN ORFNames=CRT60_12285 {ECO:0000313|EMBL:PGH57234.1};
OS Azospirillum palustre.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=2044885 {ECO:0000313|EMBL:PGH57234.1, ECO:0000313|Proteomes:UP000225379};
RN [1] {ECO:0000313|Proteomes:UP000225379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2 {ECO:0000313|Proteomes:UP000225379};
RA Kravchenko I.K., Grouzdev D.S.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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:PGH57234.1}.
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DR EMBL; PDKW01000040; PGH57234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B8B7H3; -.
DR OrthoDB; 9815791at2; -.
DR Proteomes; UP000225379; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd08192; MAR-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; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; ALCOHOL DEHYDROGENASE; 1.
DR PANTHER; PTHR11496:SF102; ALCOHOL DEHYDROGENASE 4; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR SUPFAM; SSF56796; Dehydroquinate synthase-like; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 13..377
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 388 AA; 41198 MW; 4990CF2C8EA00B08 CRC64;
MQSGVYEFLA QDRVIYGRPA AEAVAETAGR LGKSRLLIVA SRTLSRSTGV VSAIREALGD
RCIGVFDSCV EHVPRASVLA LAGEVRRLQP DLIVTVGGGT PMDTVKVTLV ALAEGIADEA
GFDAVRIRVA EDGTRIVPAV KDLPLRQIIV PTTLSGAEFS NLGGATDVTR QVKDLYTGRH
IGGQVVILDP AVTVHTPDRL WLSTGIRAVD HAVETVCSRK PQPFTDATCL HGLGMLARSL
RVNQAEPDDL DARLESQLGV WLASTGLGRV EWGASHGIGH QLGAVANVPH GHCSCVMLPS
VLRWNREVNA DRQALVARAL GREDGDAAAA VAGLVRDLGQ PGSLREVGVT RDHFAAIAAG
AMQNMMVRSN PRPITGEADI RDILELAW
//