ID A0A163ZD12_9BRAD Unreviewed; 497 AA.
AC A0A163ZD12;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Glycolate oxidase subunit GlcD {ECO:0000313|EMBL:KZD23313.1};
GN ORFNames=A4A58_08030 {ECO:0000313|EMBL:KZD23313.1};
OS Tardiphaga robiniae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Tardiphaga.
OX NCBI_TaxID=943830 {ECO:0000313|EMBL:KZD23313.1, ECO:0000313|Proteomes:UP000076574};
RN [1] {ECO:0000313|EMBL:KZD23313.1, ECO:0000313|Proteomes:UP000076574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vaf07 {ECO:0000313|EMBL:KZD23313.1,
RC ECO:0000313|Proteomes:UP000076574};
RA Kopat V., Chirak E., Kimeklis A., Andronov E.;
RT "Microsymbionts genomes from the relict species Vavilovia formosa (Stev.)
RT Fed.";
RL Submitted (MAR-2016) 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:KZD23313.1}.
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DR EMBL; LVYV01000012; KZD23313.1; -; Genomic_DNA.
DR RefSeq; WP_068733583.1; NZ_LVYV01000012.1.
DR AlphaFoldDB; A0A163ZD12; -.
DR STRING; 943830.A4A58_08030; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000076574; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000076574}.
FT DOMAIN 50..228
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 497 AA; 52931 MW; 5C03364BCFA81A79 CRC64;
MTIMMPAADQ AVLARREAII AALRKLVPGE GVISSAAEML PYESDGLMAY RQPPMVVVLP
DTTEQVSKVL KYCHENGIKV VPRGSGTSLS GGALPLADAV LLGLGKFKRV REIDFDNRAV
VVEPGVTNLA ISQAVAHAGF YYAPDPSSQI ACSIGGNVAE NSGGVHSLKY GMTTNNLLGC
EIVLMSGEVI RVGGKTAETS GYDLMGIITG SEGLLGVITE ITVRILQKPE TARALMIGFA
EVEHAGQCVA DVISAGIIPG GMEMMDKPAI HAAEAFVHAG YPLDVEALLI IELDGPGVEV
DELIKRVEKI ALGCGSTTCQ ISTSEQERLL FWSGRKAAFP AVGRISPDYL CMDGTIPRAA
LPLVLRRMKE MSAKYGLGVA NVFHAGDGNL HPLILYDANK PGELQLAEDF GADILRLCVE
VGGVLTGEHG VGIEKRDLMP EMFSEVDLNQ QQRIKCAFDA QGLLNPGKVF PTLHRCAELG
RVHVHGGKLA FPDLPRF
//
