ID K9YBY1_HALP7 Unreviewed; 493 AA.
AC K9YBY1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Glycolate oxidase, subunit GlcD {ECO:0000313|EMBL:AFZ44359.1};
DE EC=1.1.2.4 {ECO:0000313|EMBL:AFZ44359.1};
GN OrderedLocusNames=PCC7418_2205 {ECO:0000313|EMBL:AFZ44359.1};
OS Halothece sp. (strain PCC 7418) (Synechococcus sp. (strain PCC 7418)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Halothecacae; Halothece cluster; Halothece.
OX NCBI_TaxID=65093 {ECO:0000313|EMBL:AFZ44359.1, ECO:0000313|Proteomes:UP000010481};
RN [1] {ECO:0000313|Proteomes:UP000010481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7418 {ECO:0000313|Proteomes:UP000010481};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP003945; AFZ44359.1; -; Genomic_DNA.
DR RefSeq; WP_015226234.1; NC_019779.1.
DR AlphaFoldDB; K9YBY1; -.
DR STRING; 65093.PCC7418_2205; -.
DR KEGG; hao:PCC7418_2205; -.
DR PATRIC; fig|65093.3.peg.2333; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_3; -.
DR Proteomes; UP000010481; Chromosome.
DR GO; GO:0009339; C:glycolate oxidase complex; IEA:InterPro.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:InterPro.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
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; IPR004490; GlcD.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR00387; glcD; 1.
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 Oxidoreductase {ECO:0000313|EMBL:AFZ44359.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010481}.
FT DOMAIN 48..226
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 493 AA; 52573 MW; DEE6E5197211415A CRC64;
MLKSLFRSSP QDPWQPIVKA LTNVVGKDGI VQRKDELLTY ECDGLASYRQ RPKIVVLPRS
TEQVAKVVQI CDQYDLPWVA RGAGTGLSGG ALPLENGVLI VTARMNEILE TDLENQRVVV
QPGVINNWVT QAVSGKGFYY APDPSSQIIC SIGGNVAENS GGVHCLKYGV TTNHVLGLKI
VTPDGSIVDI GGTVPEMPGY DLTGLFVGSE GTLGIATEIT LRILKTPESV AVLLADFESI
EAAADGVAAI IGDGIIPAGM EMMDNLTINA VEDVVGAGLY PRDAGAILLV ELDGSEVEVS
GNIERTARIC EENGARGTTI AHDAEKRAKL WKGRKAAFAA AGHLSPDYFV QDGVIPRTQL
ATVLRDIEAL SEESGYRIAN VFHAGDGNLH PLILYNESVP GDLEKVEEIG GKILKRCVEA
GGSISGEHGI GADKNCYMSE MFSAIDLETM QYVRAAFNPK GLANPTKLFP TPRTCGEAAN
AQKTAQYQGA QFY
//
