ID E8LBD7_9FIRM Unreviewed; 466 AA.
AC E8LBD7;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Putative glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:EFY05823.1};
GN ORFNames=HMPREF9443_00148 {ECO:0000313|EMBL:EFY05823.1};
OS Phascolarctobacterium succinatutens YIT 12067.
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Phascolarctobacterium.
OX NCBI_TaxID=626939 {ECO:0000313|EMBL:EFY05823.1, ECO:0000313|Proteomes:UP000004923};
RN [1] {ECO:0000313|EMBL:EFY05823.1, ECO:0000313|Proteomes:UP000004923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12067 {ECO:0000313|EMBL:EFY05823.1,
RC ECO:0000313|Proteomes:UP000004923};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2011) 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:EFY05823.1}.
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DR EMBL; AEVN01000006; EFY05823.1; -; Genomic_DNA.
DR RefSeq; WP_009144544.1; NZ_GL830848.1.
DR AlphaFoldDB; E8LBD7; -.
DR GeneID; 78523403; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_9; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000004923; 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 InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
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:SF2; 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:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000004923}.
FT DOMAIN 44..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 466 AA; 51221 MW; B3F1C05176A53250 CRC64;
MSNYNSVTPE FIDELKTLLG EKYVKTDADT LDRYKTDEEA DERCFHLPDV VVIPANAEEI
AGVVKLCNKY LIPLTVRGGG TGIVDGAIAD KGGVVLLMER LNKIIELNKE GLYMVAQAGV
RTLDIQAAAK AENLLYAGDP SSSDSCQIGG NLATNAGGIK AVRYGVTRNQ VYAVQIVTPY
GDIVDLGSPL KKCSTGYCME QLVIGSEGTL GIITQVTLKL QPLPPYKIDM LAIFHDQMAA
IGVVPQLVKA GIDPTSIEYM DNPNVRTTSE YLEFPGAPHI EDGIYVIITI ETFNEDELDM
KMEQASDICE AAGAVDVLEA DERIWSMRRN CLESVSLISK VCTTDDVVVP VDEMSDMIQY
IIKTVAKYPF PLRINAHIGD GNLHIVLCKL DLSDEEWESE LSRFTEEVYT YAYAHGGRLS
GEHGIGSKKA HFLERFTPGG ELELMRKIKK AWDPNNILNP GKVFNL
//
