ID A0A0R2N1S4_9LACO Unreviewed; 464 AA.
AC A0A0R2N1S4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:KRO17699.1};
GN ORFNames=IV56_GL002185 {ECO:0000313|EMBL:KRO17699.1};
OS Lacticaseibacillus saniviri JCM 17471 = DSM 24301.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1293598 {ECO:0000313|EMBL:KRO17699.1, ECO:0000313|Proteomes:UP000050969};
RN [1] {ECO:0000313|EMBL:KRO17699.1, ECO:0000313|Proteomes:UP000050969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24301 {ECO:0000313|EMBL:KRO17699.1,
RC ECO:0000313|Proteomes:UP000050969};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRO17699.1}.
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DR EMBL; JQCE01000009; KRO17699.1; -; Genomic_DNA.
DR RefSeq; WP_056992556.1; NZ_JQCE01000009.1.
DR AlphaFoldDB; A0A0R2N1S4; -.
DR STRING; 1293598.IV56_GL002185; -.
DR PATRIC; fig|1293598.4.peg.2287; -.
DR Proteomes; UP000050969; 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:UP000050969}.
FT DOMAIN 45..224
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 464 AA; 50148 MW; E7642E243BBF7088 CRC64;
MATFVAYSND EILADLKQNV APDKVLTDLA DLQKHENDAY GVNTATGLPL AFIKATSVAD
IQGVLKTARK FHIPVVPQTT ATSTVSGSDA IANSFILSTA SMNHIKTIDV ADQLAVVEPG
VINQTLDTEA RKQGMFYAPD PGSKKISSIG GNAATNAGGM STVRYGATKD SILGLKVVLA
DGREIKVGSQ SLKQAFGYNL TQLFVGSEGT LGIITEITVR LFPIPLGDAI TGMAFFKDMS
TLAQAVNEIR ASGTYPTMLE ALDADTVEAL DRYEKTHYAQ NSGAMLILKL DSSTDAALKV
IEDILNKYGA QNLQLTTDAD ESETIMQLRR DMLPAIFANG QHVMEDMAVP LSKLAELMDY
IKQVAADLNL EIYTAGHAGD GNVHPTIIWP EDQPDIPENV QLGLQRMFRK TLELGGTISG
EHAVGVLKNQ WNNEELGEDV DMLQHQIKAV FDPMNILNPK RKIN
//
