ID A0A0G3HA18_9CORY Unreviewed; 979 AA.
AC A0A0G3HA18;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=FAD/FMN-dependent dehydrogenase {ECO:0000313|EMBL:AKK08738.1};
GN ORFNames=CTEST_06500 {ECO:0000313|EMBL:AKK08738.1};
OS Corynebacterium testudinoris.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=136857 {ECO:0000313|EMBL:AKK08738.1, ECO:0000313|Proteomes:UP000035540};
RN [1] {ECO:0000313|EMBL:AKK08738.1, ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|EMBL:AKK08738.1,
RC ECO:0000313|Proteomes:UP000035540};
RX PubMed=26227591;
RA Ruckert C., Kriete M., Jaenicke S., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium testudinoris
RT DSM 44614, Recovered from Necrotic Lesions in the Mouth of a Tortoise.";
RL Genome Announc. 3:e00784-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44614 {ECO:0000313|Proteomes:UP000035540};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium testudinoris DSM 44614,
RT recovered from necrotic lesions in the mouth of a tortoise.";
RL Submitted (MAY-2015) 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; CP011545; AKK08738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3HA18; -.
DR STRING; 136857.CTEST_06500; -.
DR KEGG; cted:CTEST_06500; -.
DR PATRIC; fig|136857.5.peg.1291; -.
DR Proteomes; UP000035540; 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 InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 1.
DR Pfam; PF02754; CCG; 2.
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:UP000035540}.
FT DOMAIN 70..298
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT DOMAIN 562..593
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 979 AA; 105884 MW; 06D8C001FEB5425F CRC64;
MRGMRKLFSP QPQTIGRPKG ATSQADAVSE RYLEGTPQQV LDELASIVGK DNVLGRLSDL
VRYASDAGPY RTVPSVVVRP RNAQDLAGLM AYARQNNRHL VFRAAGTSLN GQAMTDDILV
DVKTHFGGMK VLDEGARLWS RPGVILGDAQ AVLARHGFML GPDPGSTSVC TIGGVIADNA
GGMRCSVPRD TYHSLESATI VLPSGTVIDT AAEDADEQLA RLEPEIHAGL IALREEIRGD
DELVALLQRK FSIRNTNGLR LDAFLDEERP VDILLRLMVS SEGTLGAVTE SVIRTIPLPR
KKAVAWVMLP DLRQAASYVH ALMETGAEAC ELLVAPVLKR AVGNFPTAPA EWADFDENAA
ALLLEVGGTD EADLADAIKR AEAVLINAEL LSPLRFDDTP DGMRGAWSIR NGLFGLIGAD
RPQGSALITE DVCFPPADVG AGAADLLDLL ASYGYPEMVM GHAAFGNLHF FLLPRFDIEE
EREAYANFLD DLTDLVIGKY QGSLKAEHGT GVNMAPFLQR EWGDRAWELM WDVKDLLDPA
GILAPNVKLT RDPLVHLQNF KSFPQVEEEI NQCVECGFCE PVCPSRHITV TPRQRIVLRR
EMARQPEGSK VLEKLQEEFQ YDGIDMCAVD GTCSIPCPIS IDTGAAMKQL RAQQHSSGAK
KVALSTAKNW AAVEKTARVG MSVAEKLPTP LLRGAANLGR TLINEDLLPT VPGPLPDAAA
SHLPLTTREG ASALYFPACV NRIFGQPGDA SPDHLSLPES VVELGRRSGR PVWIPEGVAG
DCCGTPWSSK GYKEGFNYQA QQIARDLVEW SDNGALPVVV DAASCTHGLL EQVPHALDGE
LAEQFAQLQI LDVVEWLHSE VLPGLPIVRT VGRAAVHPTC STMHMGINDQ LRDLTQAAAD
ELVVPERATC CGTAGDRVLL HPELVKSATS EEMAELTGHF DAFVSDNRTC EMGLEMTSGH
TYESIAVLLE KVSRPVVTP
//
