ID C7RC96_KANKD Unreviewed; 463 AA.
AC C7RC96;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ACV26888.1};
GN OrderedLocusNames=Kkor_1476 {ECO:0000313|EMBL:ACV26888.1};
OS Kangiella koreensis (strain DSM 16069 / KCTC 12182 / SW-125).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Kangiellales; Kangiellaceae;
OC Kangiella.
OX NCBI_TaxID=523791 {ECO:0000313|EMBL:ACV26888.1, ECO:0000313|Proteomes:UP000001231};
RN [1] {ECO:0000313|EMBL:ACV26888.1, ECO:0000313|Proteomes:UP000001231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16069 / KCTC 12182 / SW-125
RC {ECO:0000313|Proteomes:UP000001231};
RX PubMed=21304661; DOI=10.4056/sigs.36635;
RA Han C., Sikorski J., Lapidus A., Nolan M., Glavina Del Rio T., Tice H.,
RA Cheng J.F., Lucas S., Chen F., Copeland A., Ivanova N., Mavromatis K.,
RA Ovchinnikova G., Pati A., Bruce D., Goodwin L., Pitluck S., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Brettin T., Goker M., Tindall B.J., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Kangiella koreensis type strain (SW-125).";
RL Stand. Genomic Sci. 1:226-233(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; CP001707; ACV26888.1; -; Genomic_DNA.
DR RefSeq; WP_012801402.1; NC_013166.1.
DR AlphaFoldDB; C7RC96; -.
DR STRING; 523791.Kkor_1476; -.
DR KEGG; kko:Kkor_1476; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_4_1_6; -.
DR InParanoid; C7RC96; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000001231; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 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; IPR016167; FAD-bd_PCMH_sub1.
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; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Reference proteome {ECO:0000313|Proteomes:UP000001231}.
FT DOMAIN 37..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 463 AA; 50894 MW; FDD0569BC0961ABB CRC64;
MSSDTYIAQL RTLLDDDCLL TDKDSLDHYG KDWTNIKQPA PLAIALPKTT EQVQALILWA
NDNQIAIVPS GGRTGLSGGA VAANGELVVA LDKMNKVIEF NPGSQQVKCQ AGAITEQIQQ
FAEDNDLYYP VDFASSGSSQ IGGNIATNAG GIKVIRYGLT RDWVQGLTVV TGKGDILELN
KGLVKNATGY DLRHLFIGSE GTLGIVTEAT LKLTRKPVNL TVLLLAIPNL DSLMPILQQF
QKAVDLTAFE FFSDEALEKV MAHHNLACPV QQRAPYYCLL EFDAASEDIL EAALAEFETG
LGNEQILDGT MSQSQQQVED LWKYREFISE TISGRKPYKN DISVTPEKIT KFLTGVNDIV
AKDYPDFEVI WFGHIGDGNL HLNILAPEDM DYQEFTESCE QVNPKIFTLL QELGGSISAE
HGVGLLKKPY LNFTRSDTEI SYLKAIKHAF DPKGIMNPGK VID
//
