ID A0A124G7X5_9ACTN Unreviewed; 463 AA.
AC A0A124G7X5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=ADL15_44960 {ECO:0000313|EMBL:KUL23967.1};
OS Actinoplanes awajinensis subsp. mycoplanecinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL23967.1, ECO:0000313|Proteomes:UP000053244};
RN [1] {ECO:0000313|EMBL:KUL23967.1, ECO:0000313|Proteomes:UP000053244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL23967.1,
RC ECO:0000313|Proteomes:UP000053244};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUL23967.1}.
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DR EMBL; LLZH01000326; KUL23967.1; -; Genomic_DNA.
DR RefSeq; WP_067705770.1; NZ_LLZH01000326.1.
DR AlphaFoldDB; A0A124G7X5; -.
DR OrthoDB; 9770306at2; -.
DR Proteomes; UP000053244; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000053244}.
FT DOMAIN 35..214
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 463 AA; 49945 MW; 947D734B36F2ED63 CRC64;
MTLSKELAEI VGAEHCLTGT DIGARYAQDL WGSDRKGDPQ LVVRPGGTAE VAAILRLCHE
RGVPVVPQGG MTGLVSGGVP GADEVVLSLE RMNQVEELDR STRTMTVQAG CTLAAVQDLA
AEHDLMFPLD VAPRTAATIG GAIATNAGGL RVLLYGMMRE LVLGLEVVLA DGTIVNGLHK
LVKNNAGHDL KQLFIGTEGT LGVVTRATLR LRPAPQCRFA AMCGVADLDA ALDLLHRLQA
ALPGMVSAFE AVWDDAYEVL LPVRDEITLP LQKVHPIAVL IEVSGVDAGK DLDRLHRALD
DCADIVGEST VAATAEQVGL LWQARERIPK QILQMQPLFG FDISLPAGLL DQYLSEVREE
LRGHWPAVKL LVFGHLGDGN VHIAVVTGEQ TRDRKAVVEH IIYRAVRRHG GSISAEHGIG
FEKRPYLHYS RTAEEIALMR LLKQTLDPRG ILSPGRILDE ASQ
//
