ID A0A0S9NWU0_9BURK Unreviewed; 493 AA.
AC A0A0S9NWU0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Glycolate oxidase subunit GlcD {ECO:0000313|EMBL:KQP49773.1};
GN ORFNames=ASF44_04125 {ECO:0000313|EMBL:KQP49773.1};
OS Pseudorhodoferax sp. Leaf274.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP49773.1, ECO:0000313|Proteomes:UP000051759};
RN [1] {ECO:0000313|EMBL:KQP49773.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP49773.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP49773.1, ECO:0000313|Proteomes:UP000051759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf274 {ECO:0000313|EMBL:KQP49773.1,
RC ECO:0000313|Proteomes:UP000051759};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KQP49773.1}.
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DR EMBL; LMNA01000001; KQP49773.1; -; Genomic_DNA.
DR RefSeq; WP_056897857.1; NZ_LMNA01000001.1.
DR AlphaFoldDB; A0A0S9NWU0; -.
DR STRING; 1736318.ASF44_04125; -.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000051759; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF1; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000051759}.
FT DOMAIN 46..224
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 493 AA; 51849 MW; A2043D8C0F286E51 CRC64;
MAALAAPTAP PPAETLAALR RVLPAHALLS QPEDTTPYEC DGLTAYRQRP MAVALPETYA
QVQAVLKTCH ALGVPVVARG AGTGLSGGAM PHAQGVTLSM AKFNKILHMD PVGRTAVVQC
GVRNLAISEA AAPHGLYYAP DPSSQIACTI GGNVAENSGG VHCLKYGLTV HNVLQITGFT
AEGEPVTFGS AALDTPGLDL LALAIGSEGM LAVATEVTVK LVPKPLLARC IMASFDDMRK
AGDAVAAVIA AGIIPAGLEM MDKPMTAAVE DFVRAGYDLT AEAILLCESD GTPEEVEEEI
GRMSAVLRGC GATAITVSQN EAERLRFWSG RKNAFPASGR ISPDYMCMDS TIPRKRLADI
LLAIAAMEKK YGLRCANVFH AGDGNLHPLI LFDANDPDQL HRCELFGADI LETSVAMGGT
VTGEHGVGVE KLNSMCVQFS AEENAQMLGI KHAFDTKGLL NPGKVIPTLN RCAEYGKMLV
RGGKIAHPDL PRF
//
