ID K2C9X1_9BACT Unreviewed; 462 AA.
AC K2C9X1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=ACD_42C00114G0004 {ECO:0000313|EMBL:EKD77928.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD77928.1};
RN [1] {ECO:0000313|EMBL:EKD77928.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKD77928.1}.
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DR EMBL; AMFJ01017385; EKD77928.1; -; Genomic_DNA.
DR AlphaFoldDB; K2C9X1; -.
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;
FT DOMAIN 38..217
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 462 AA; 51700 MW; 6FA00D9DF93C03C8 CRC64;
MENNFIISAV MTIFSKDRVL FDYQSILIYG KDLTDVLPPP HALCVVFPQD KNELVSLVHF
ANEHRLSLVP SGGRTGYSGG AVAKQNDIIV SFEKMNHIVD FNAADKTLHC EAGVTLKAIQ
DYAKQLDLFY PVDFASAAEC QIGGNIATNA GGLHVIRYGS TRQWVMGLTV ITGRGDILGC
NKGLVKNATG YDFRHLFIGS EGTLGFITHA ILKLTALPKK TKVILFSVSN NQAITILLSV
LQQAVSLIAF EFFCHTAMQC VMQAEQIAFP FQKNTDFYGL FEYESDDTVD LIIEKILQDQ
LNKNNISEIL MSHHEKEANH LWRYRKGISR SLKKYFPYKF DLAVLPSTIF SFMRAAADLL
RNKYAALETV WFGHVGDGNL HVNVLKPETV SEKDFAVRCA EISETIYAVI QHFNGSICAE
HGVGLLKKPY LHYSKSDSEI QYMRGIKNIF DPNHVMNPGK LI
//
