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
//