ID A0A1M6S7H6_9BURK Unreviewed; 358 AA.
AC A0A1M6S7H6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=maleylacetate reductase {ECO:0000256|ARBA:ARBA00012005};
DE EC=1.3.1.32 {ECO:0000256|ARBA:ARBA00012005};
GN ORFNames=SAMN05192548_102145 {ECO:0000313|EMBL:SHK40619.1};
OS Paraburkholderia terricola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=169427 {ECO:0000313|EMBL:SHK40619.1, ECO:0000313|Proteomes:UP000184395};
RN [1] {ECO:0000313|EMBL:SHK40619.1, ECO:0000313|Proteomes:UP000184395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 20594 {ECO:0000313|EMBL:SHK40619.1,
RC ECO:0000313|Proteomes:UP000184395};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxoadipate + NAD(+) = H(+) + maleylacetate + NADH;
CC Xref=Rhea:RHEA:16981, ChEBI:CHEBI:15378, ChEBI:CHEBI:15775,
CC ChEBI:CHEBI:16468, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.3.1.32;
CC Evidence={ECO:0000256|ARBA:ARBA00000519};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxoadipate + NADP(+) = H(+) + maleylacetate + NADPH;
CC Xref=Rhea:RHEA:16985, ChEBI:CHEBI:15378, ChEBI:CHEBI:15775,
CC ChEBI:CHEBI:16468, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.32;
CC Evidence={ECO:0000256|ARBA:ARBA00001753};
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000256|ARBA:ARBA00007358}.
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DR EMBL; FRAB01000021; SHK40619.1; -; Genomic_DNA.
DR RefSeq; WP_073430259.1; NZ_FRAB01000021.1.
DR AlphaFoldDB; A0A1M6S7H6; -.
DR STRING; 169427.SAMN05192548_102145; -.
DR OrthoDB; 3812122at2; -.
DR Proteomes; UP000184395; Unassembled WGS sequence.
DR GO; GO:0018506; F:maleylacetate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd08177; MAR; 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 InterPro; IPR034786; MAR.
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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 14..338
FT /note="Alcohol dehydrogenase iron-type/glycerol
FT dehydrogenase GldA"
FT /evidence="ECO:0000259|Pfam:PF00465"
SQ SEQUENCE 358 AA; 37645 MW; 6BD69E1D782821A5 CRC64;
MQKREFVYQA RAGRVVFGPG SLQHLEREML ELKSERALIL CSPEQKEMGE AVATRLGARA
AGVFDRAVMH VPLELAKEGR ALARELNADC AIAVGGGSTI GLGKAIALAS GLPIIAVPTT
YAGSEMTPIY GITDAGLKKT GTDPRVLPKI VIYDADLTMS LPIALSVTSG INAIAHAAEA
LYSRDANPVT SLMAEEGIAA FARALPAIVA DPQDVEARAD AQYGAWLCGT VLGSVGMALH
HKLCHTLGGS FNLPHAQTHT IVLPHALAYN RHAAPEAMER IARALGSEDA AIGVYELAKR
CGAPLALKDI GMSPEDVSKA ADIASSNPYW NPRPIQHDAL LKLLQNAFDG VAPRAASA
//