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Database: UniProt
Entry: A0A3G6J649_9CORY
LinkDB: A0A3G6J649_9CORY
Original site: A0A3G6J649_9CORY 
ID   A0A3G6J649_9CORY        Unreviewed;       983 AA.
AC   A0A3G6J649;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Glycolate oxidase subunit GlcD {ECO:0000313|EMBL:AZA13537.1};
GN   ORFNames=CCHOA_05685 {ECO:0000313|EMBL:AZA13537.1};
OS   Corynebacterium choanae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1862358 {ECO:0000313|EMBL:AZA13537.1, ECO:0000313|Proteomes:UP000269019};
RN   [1] {ECO:0000313|EMBL:AZA13537.1, ECO:0000313|Proteomes:UP000269019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=200CH {ECO:0000313|EMBL:AZA13537.1,
RC   ECO:0000313|Proteomes:UP000269019};
RA   Kleinhagauer T., Glaeser S.P., Spergser J., Ruckert C., Kaempfer P.,
RA   Busse H.-J.;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP033896; AZA13537.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G6J649; -.
DR   KEGG; ccho:CCHOA_05685; -.
DR   OrthoDB; 9770306at2; -.
DR   Proteomes; UP000269019; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
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; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR   Pfam; PF02754; CCG; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269019}.
FT   DOMAIN          67..295
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          559..590
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   983 AA;  106002 MW;  4068AA1088B1E8A0 CRC64;
     MKKIASATPE QYGRPAGATA QPDRVADDRA SGADPQTIAD LAAIVGQCNV AGRISDVVRY
     ASDGSPYRAV PQVVVKPRNA QDLSAIMRWA KRNDRKLVFR AGGSSLNGQA MAKDVMVDVK
     THFTGMKVLD GGKRLWSRPG VVLGDAQAVL GRHGYMLGPD PGSTTVACLG GIVADNSGGM
     RCTVEQDSYH CLEDAVFVLP SGTIVDTRDP QAAAKLTTAE PRLVAGLLQL RDEIRSDAAL
     VTMLREKFAI RNTNGLRLDA FLDEDSPERI LLKLLVGSEG IFGCLTEVVM RTVPVPKYKA
     CAWLILPDVK AAANYVAPLV AAGATACELL VAPMMKEAIG NFRDARESWA DMPDEAGALL
     LELGATTQEG LAAQIDKVHE VLAAATLLEP LSFFTDPQAM RGAWQIRSGL FGLVGKLRRQ
     GSTMITEDVC FPPAKVGEGS AALVDLLREY GFDATVMGHA TFGNLHFFIA PKLDVPAEKE
     NYAKFIEALA KLVIEDFGGS LKAEHGTGVN MAPFVEYEWG SQAYELFWRV KELIDPALLL
     APDVKLTRNQ QIHLQGLKSF PIVEEEIADC VECGMCEPVC PSRHVSVTPR HRIALRREMS
     RQPEGSPVLR QLQEEYDYDA VQLCAADASC AIACPVSIDT GALMKKLREK QHNQATQSAA
     LHTAKHYDLV EKAARASMMA ASRVGSTVGF GLLQAAADAG RTVISKDLLP TVPGPLPQAA
     PAQLPSTTRE GATAVYVPAC INRIFGNPHG AARDQLTVPQ AIVELGRRSG APVWIPDHLT
     GLCCGTPWSS KGYTDGFYHA ASKMVTALLE FTNEGELPVI IDAASCTHGL VGQVRTKLHN
     YDPQLAARFA KVEVLDVVQW LEREVIDHLP ITTTLGNTVV HPTCSTMHMG IDDALLRLAQ
     RVTTSAVIPD GARCCGTAGD RVLLHPELVE SATREERDSL NDGFEYFVSD NRTCEMGLEM
     IAGKPYQSIA CLLERASRPL MSS
//
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