LIGXC_SPHSK
ID LIGXC_SPHSK Reviewed; 105 AA.
AC G2IN77;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=5,5'-dehydrodivanillate O-demethylase ferredoxin subunit {ECO:0000305};
DE Short=DDVA O-demethylase ferredoxin subunit {ECO:0000305};
DE EC=1.14.13.- {ECO:0000269|PubMed:25217011};
GN Name=ligXc {ECO:0000303|PubMed:25217011};
GN ORFNames=SLG_08500 {ECO:0000312|EMBL:BAK65525.1};
OS Sphingobium sp. (strain NBRC 103272 / SYK-6).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=627192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=22207743; DOI=10.1128/jb.06254-11;
RA Masai E., Kamimura N., Kasai D., Oguchi A., Ankai A., Fukui S.,
RA Takahashi M., Yashiro I., Sasaki H., Harada T., Nakamura S., Katano Y.,
RA Narita-Yamada S., Nakazawa H., Hara H., Katayama Y., Fukuda M.,
RA Yamazaki S., Fujita N.;
RT "Complete genome sequence of Sphingobium sp. strain SYK-6, a degrader of
RT lignin-derived biaryls and monoaryls.";
RL J. Bacteriol. 194:534-535(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=NBRC 103272 / SYK-6;
RX PubMed=25217011; DOI=10.1128/aem.02236-14;
RA Yoshikata T., Suzuki K., Kamimura N., Namiki M., Hishiyama S., Araki T.,
RA Kasai D., Otsuka Y., Nakamura M., Fukuda M., Katayama Y., Masai E.;
RT "Three-component O-demethylase system essential for catabolism of a lignin-
RT derived biphenyl compound in Sphingobium sp. strain SYK-6.";
RL Appl. Environ. Microbiol. 80:7142-7153(2014).
CC -!- FUNCTION: Involved in the catabolism of 5,5'-dehydrodivanillate (DDVA),
CC an intermediate in the biodegradation of lignin. Part of a three-
CC component monooxygenase that catalyzes the O-demethylation of DDVA,
CC leading to the formation of 2,2',3-trihydroxy-3'-methoxy-5,5'-
CC dicarboxybiphenyl (OH-DDVA). LigXc probably functions as an
CC intermediate electron transfer protein between LigXd and LigXa.
CC {ECO:0000269|PubMed:25217011}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,5'-dehydrodivanillate + H(+) + NADH + O2 = 2,2',3-
CC trihydroxy-3'-methoxy-5,5'-dicarboxybiphenyl + formaldehyde + H2O +
CC NAD(+); Xref=Rhea:RHEA:57008, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16842, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:141401, ChEBI:CHEBI:141402;
CC Evidence={ECO:0000269|PubMed:25217011};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00465};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00465};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:25217011};
CC Temperature dependence:
CC Optimum temperature is 25-30 degrees Celsius.
CC {ECO:0000269|PubMed:25217011};
CC -!- SUBUNIT: Monomer. The three-component monooxygenase is composed of an
CC oxygenase (LigXa), a ferredoxin (LigXc) and a ferredoxin reductase
CC (LigXd). {ECO:0000269|PubMed:25217011}.
CC -!- DISRUPTION PHENOTYPE: Disruption mutant shows growth defect on DDVA.
CC {ECO:0000269|PubMed:25217011}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
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DR EMBL; AP012222; BAK65525.1; -; Genomic_DNA.
DR RefSeq; WP_014075176.1; NC_015976.1.
DR AlphaFoldDB; G2IN77; -.
DR SMR; G2IN77; -.
DR STRING; 627192.SLG_08500; -.
DR EnsemblBacteria; BAK65525; BAK65525; SLG_08500.
DR KEGG; ssy:SLG_08500; -.
DR eggNOG; COG0633; Bacteria.
DR HOGENOM; CLU_082632_5_1_5; -.
DR OrthoDB; 1837979at2; -.
DR Proteomes; UP000001275; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Monooxygenase; NAD; Oxidoreductase; Reference proteome; Transport.
FT CHAIN 1..105
FT /note="5,5'-dehydrodivanillate O-demethylase ferredoxin
FT subunit"
FT /id="PRO_0000445224"
FT DOMAIN 2..105
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 40
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 46
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 86
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
SQ SEQUENCE 105 AA; 11322 MW; 49CC09008DA2F981 CRC64;
MAQLKVVTRD GSLHEFEAPD GYTVMEAIRD QGIDELLAIC GGCCSCATCH VFVEEAFLDK
LPPLKGDEDD LLDSSDHRQA NSRLSCQLPI GPELGGMTVT IAPED
