GRAC_RHIS5
ID GRAC_RHIS5 Reviewed; 351 AA.
AC A1IIX4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Maleylacetate reductase {ECO:0000303|PubMed:17158677};
DE EC=1.3.1.32 {ECO:0000269|PubMed:17158677};
GN Name=graC {ECO:0000303|PubMed:17158677};
OS Rhizobium sp. (strain MTP-10005).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=267998;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RC STRAIN=MTP-10005;
RX PubMed=17158677; DOI=10.1128/jb.01675-06;
RA Yoshida M., Oikawa T., Obata H., Abe K., Mihara H., Esaki N.;
RT "Biochemical and genetic analysis of the gamma-resorcylate (2,6-
RT dihydroxybenzoate) catabolic pathway in Rhizobium sp. strain MTP-10005:
RT identification and functional analysis of its gene cluster.";
RL J. Bacteriol. 189:1573-1581(2007).
RN [2]
RP SUBUNIT, AND CRYSTALLIZATION.
RC STRAIN=MTP-10005;
RX PubMed=18678945; DOI=10.1107/s1744309108022537;
RA Fujii T., Goda Y., Yoshida M., Oikawa T., Hata Y.;
RT "Crystallization and preliminary X-ray diffraction studies of maleylacetate
RT reductase from Rhizobium sp. strain MTP-10005.";
RL Acta Crystallogr. F 64:737-739(2008).
RN [3] {ECO:0007744|PDB:3W5S}
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF CYS-242; HIS-243 AND TYR-326.
RC STRAIN=MTP-10005;
RX PubMed=27040018; DOI=10.1002/prot.25046;
RA Fujii T., Sato A., Okamoto Y., Yamauchi T., Kato S., Yoshida M., Oikawa T.,
RA Hata Y.;
RT "The crystal structure of maleylacetate reductase from Rhizobium sp. strain
RT MTP-10005 provides insights into the reaction mechanism of enzymes in its
RT original family.";
RL Proteins 84:1029-1042(2016).
CC -!- FUNCTION: Involved in the gamma-resorcylate (2,6-dihydroxybenzoate)
CC catabolism (PubMed:17158677). Catalyzes the reduction of maleylacetate
CC to 3-oxoadipate (PubMed:17158677, PubMed:27040018).
CC {ECO:0000269|PubMed:17158677, ECO:0000269|PubMed:27040018}.
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:0000269|PubMed:17158677, ECO:0000269|PubMed:27040018};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16983;
CC Evidence={ECO:0000269|PubMed:17158677, ECO:0000269|PubMed:27040018};
CC -!- PATHWAY: Aromatic compound metabolism. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18678945,
CC ECO:0000269|PubMed:27040018}.
CC -!- INDUCTION: Induced in the presence of gamma-resorcylate.
CC {ECO:0000269|PubMed:17158677}.
CC -!- DOMAIN: Each subunit consists of two domains: an N-terminal NADH-
CC binding domain adopting an alpha/beta structure and a C-terminal
CC functional domain adopting an alpha-helical structure.
CC {ECO:0000269|PubMed:27040018}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AB266212; BAF44524.1; -; Genomic_DNA.
DR PDB; 3W5S; X-ray; 1.49 A; A/B=1-351.
DR PDBsum; 3W5S; -.
DR SMR; A1IIX4; -.
DR BioCyc; MetaCyc:MON-19794; -.
DR BRENDA; 1.3.1.32; 5351.
DR GO; GO:0018506; F:maleylacetate reductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd08177; MAR; 1.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR034786; MAR.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase.
FT CHAIN 1..351
FT /note="Maleylacetate reductase"
FT /id="PRO_0000454492"
FT MUTAGEN 242
FT /note="C->A: Retains 25% of wild-type specific activity."
FT /evidence="ECO:0000269|PubMed:27040018"
FT MUTAGEN 243
FT /note="H->A: Retains 0.4% of wild-type specific activity."
FT /evidence="ECO:0000269|PubMed:27040018"
FT MUTAGEN 326
FT /note="Y->A: Retains 6% of wild-type specific activity."
FT /evidence="ECO:0000269|PubMed:27040018"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:3W5S"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:3W5S"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3W5S"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:3W5S"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:3W5S"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3W5S"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3W5S"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:3W5S"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3W5S"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 161..178
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 186..208
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 213..233
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 237..249
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 253..269
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 273..283
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 314..321
FT /evidence="ECO:0007829|PDB:3W5S"
FT HELIX 334..346
FT /evidence="ECO:0007829|PDB:3W5S"
SQ SEQUENCE 351 AA; 36406 MW; 4026F49E9A38F624 CRC64;
MQPFVYTTAP ARIVFGTGSS VGVAEEIRRL GLSRALVLST PHQKGDAEAL AARLGPLAAG
VFSDAAMHTP VEVTKRAVEA YRAAGADCVV SLGGGSTTGL GKAIALRTDA PQIVIPTTYA
GSEVTPILGQ TENGVKTTLR GPEILPEVVI YDAELTLGLP VGISMTSGLN AMAHAAEALY
ARDRNPIASM MAVEGLRAMI EALPGVRMEP QDTKARETAL YGAWLCGTVL GAVGMSLHHK
LCHTLGGSLD LPHAETHAVL LPYTIAYVEQ AVPDQLAPLA ALVGGRAGTG LYDFAARLGA
PASLAALGVG GEDLDAMAEL ATANPYWCPR PVEKTAIRAL LQRAFEGARP E
