ID A0A147ENY7_9MICO Unreviewed; 543 AA.
AC A0A147ENY7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=NS354_05610 {ECO:0000313|EMBL:KTR86179.1};
OS Leucobacter chromiiresistens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1079994 {ECO:0000313|EMBL:KTR86179.1, ECO:0000313|Proteomes:UP000070810};
RN [1] {ECO:0000313|EMBL:KTR86179.1, ECO:0000313|Proteomes:UP000070810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NS354 {ECO:0000313|EMBL:KTR86179.1,
RC ECO:0000313|Proteomes:UP000070810};
RX PubMed=26793183;
RA Midha S., Bansal K., Sharma S., Kumar N., Patil P.P., Chaudhry V.,
RA Patil P.B.;
RT "Genomic Resource of Rice Seed Associated Bacteria.";
RL Front. Microbiol. 6:1551-1551(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KTR86179.1}.
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DR EMBL; LDRK01000026; KTR86179.1; -; Genomic_DNA.
DR RefSeq; WP_058593604.1; NZ_LDRK01000026.1.
DR AlphaFoldDB; A0A147ENY7; -.
DR PATRIC; fig|1079994.3.peg.1211; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000070810; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.10; FAD-linked oxidases, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR016170; Cytok_DH_C_sf.
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; PTHR11748:SF114; ARYL-ALCOHOL OXIDASE VANILLYL-ALCOHOL OXIDASE (AFU_ORTHOLOGUE AFUA_3G09500)-RELATED; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 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 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000070810}.
FT DOMAIN 61..248
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 543 AA; 60139 MW; C1B72FFD928E42CE CRC64;
MSTARTDAFG ETISHLPPGV GAEHFIAAID RMREAIGAEN VHVDDATVRQ YDDRFPVTDG
DEFRGGAVVW PGSTADVQAI VRIANEFLIP LHAFSTGRNL GYGGSSPMVT GSVLLHLGKR
MNRVLEINEK LAYAVVEPGV DYATLHRAVE ESGAQLMIDP AELDWGSVIG NTMDHGVGYT
PYGDHAMWRC GMEVVLPDGE VLRTGMGGLP ESEAWHLYAG GIGPSVEGLF EQSNYGICTR
MGMQLMPKPE SAVTFAITFP REEDLAAIME ITLPLRIGMA PIQSVPIVRN IVFDAACVSR
RDEWQQDPGP LTAEAKQRMI DALDSGYWIL YGTCYGPRWQ VDRYLEIIEG AYSQIEGARF
ETNETLPPAF GDRRADLLHA RHLLNTGVPN RHSAAVFDWF PNAGHFFYAP VSAPSGPDAA
TQFSDTQRIS DAYGKDYLAQ FIIGLREMHH ICLPLYDVTD QRSRAETLQM TRELITTGAQ
EGYGIYRTHN VLAEQVVETY RFNDHIQRAF AERIKDALDP NGILNPGKSG IWPERLRPNR
SSR
//
