ID A0A160FKM7_9BURK Unreviewed; 985 AA.
AC A0A160FKM7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pyrogallol hydroxytransferase large subunit {ECO:0000313|EMBL:ANB72999.1};
GN ORFNames=AYM40_11970 {ECO:0000313|EMBL:ANB72999.1};
OS Paraburkholderia phytofirmans OLGA172.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB72999.1, ECO:0000313|Proteomes:UP000076852};
RN [1] {ECO:0000313|EMBL:ANB72999.1, ECO:0000313|Proteomes:UP000076852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLGA172 {ECO:0000313|EMBL:ANB72999.1,
RC ECO:0000313|Proteomes:UP000076852};
RX PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT chlorocatechol degradative operon in a region of genome plasticity.";
RL Gene 586:239-247(2016).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP014578; ANB72999.1; -; Genomic_DNA.
DR RefSeq; WP_063496409.1; NZ_CP014578.1.
DR AlphaFoldDB; A0A160FKM7; -.
DR STRING; 1804984.AYM40_11970; -.
DR KEGG; buz:AYM40_11970; -.
DR Proteomes; UP000076852; Chromosome 1.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.20.25.340; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR049032; AhtL-like_N.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR Pfam; PF21423; AhtL-like_1st; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076852};
KW Transferase {ECO:0000313|EMBL:ANB72999.1}.
FT DOMAIN 146..200
FT /note="Pyrogallol hydroxytransferase large subunit-like N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF21423"
FT DOMAIN 206..711
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 842..965
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 985 AA; 110006 MW; B44367E444520F6D CRC64;
MQRHILVLIL WLMPFALRMA ARKFPSVREH LGSGHWVIQL RLRDNSLARQ LHFRNGTVSA
RWGVNTKPDA ELVFMDVATA RQMLAPTTDH AFLIDALKNF KITQGGSDEA LVWFGQLVNT
MKTGSWRTGT RMKDGTTRYV TLTNGGPVFV FVKDGKIIRT TPIDLAAEDG PSWTITARGR
QFSPARRATV SPHALSLKSL VYSDKRILYP MKRVDFDPKG ERNPQTRGTS GYERISWDEA
LDIVVGEIRR MKQEHGPGAI AMATGAHHQW GNVNYYLSAM QRFGNLIGYT RIEMSPISWE
GWYWGAMHHY GNSLRLGTPS FYGTTEDCLE HAEVIVFWSS DPESTNGVYA GFEGTERRLW
AKQLGIQFVH IDPYLTQSAQ FLGGKWLPIK PGTDSALAIA IMHEWMISGS YDEEYVASKT
TGFDEWRAYV LGEEDGTPKT PEWQEAETGI PAKDVRSLAQ LWASKKTYLA AGGLGAGFGG
ACRTETGAQW TRSLVMMMAM RGWGKPGINF GNLQIGAPQD LNFYFPGYAE GGISGDLTYT
ASAANNYCRM PHIITINPVK QSIPRQRLAE AITQGSAEGY FWDGFSAEGQ FGQYSYPKLG
HSRVHMLYRY GSSSFGTVPG SNRLVDAYRH PSLEFVVNQS VWMENEAQFA DIILPACTAL
ERDDISEWAN CGGYIQHAQS QLNHRMMIMQ HKCIEPLGES KSDYQIFLEI LTRLGYGGMY
SEGGGSELTW CERIFNSTDL PKQTTWKKFL QKGYHVVPPP KDDDKQPVDM RWFAEGRTKD
LPEANPLPGV YSTGFSQGLP TQSGKFEFVP SSLRRIEQID PARPAVNRYI NSQSGVKQRF
PLQLVTNHPV YSFHTQADGK NSHISTINEH RMNVGGYRYW VLRMSPTDAS ARGLGSGDLV
RVYNTQASVI CAIDVSQLVK DGVARGNESC GELDLIQTSV GMVDRGGCLN LLTPGRKMSE
TADGIVPNSC WVEVEKWDTT MEKAA
//
