ID A0A0Q9KJB0_9MICO Unreviewed; 471 AA.
AC A0A0Q9KJB0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN ORFNames=ASG73_11825 {ECO:0000313|EMBL:KRE36996.1};
OS Janibacter sp. Soil728.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Janibacter.
OX NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE36996.1, ECO:0000313|Proteomes:UP000051572};
RN [1] {ECO:0000313|EMBL:KRE36996.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE36996.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE36996.1, ECO:0000313|Proteomes:UP000051572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil728 {ECO:0000313|EMBL:KRE36996.1,
RC ECO:0000313|Proteomes:UP000051572};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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 oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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:KRE36996.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMRZ01000005; KRE36996.1; -; Genomic_DNA.
DR RefSeq; WP_055995244.1; NZ_LMRZ01000005.1.
DR AlphaFoldDB; A0A0Q9KJB0; -.
DR STRING; 1736393.ASG73_11825; -.
DR Proteomes; UP000051572; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.40.462.20; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42973; BINDING OXIDOREDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G17690)-RELATED; 1.
DR PANTHER; PTHR42973:SF39; FAD-BINDING PCMH-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..471
FT /note="FAD-binding PCMH-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006376938"
FT DOMAIN 68..238
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 471 AA; 49639 MW; F7E14A66676CEFC1 CRC64;
MDISRRTVIG AGAALPLTAA SSAFAAPTVT GPSPGDWADL DRTLAGSASL PGSYRYESRV
PLFDPRWDYR RPAALARILS RQDISTCITF ARDHGLTITG RSGGHSYIGA SRAAGSLVID
TRSYTKVHFP TDRAETTVQA GANLYSVHAQ ISRYGRSIPT GTCPTVGSAG LTLVGGLGVD
SRRYGLTIDR LVSATVIDGR GVIRKVDANR DPDLFWALRG GGSGAAMVAD LTYRTIPATS
MGFFNVSFPA SSTATVLRQW AVWMADQPRD TWANAHVDTA GSSISVRVFG VTPVGLEATR
AASLRRAVGI TPLSTSTTTR THLAGIRYLG GGSTTPRTRF AAGSDILRTM TSDGAEAVVA
AMRSAASRGL SASAILDPLD GAMATPAMAA TAFPWRNHVA SIQWYVGVGS SSGYAPAQDW
IAHAHDLLSA HSRGGYFGYV ESGRPMDAYF AGNYPQLAAA RLRYDPDSIL L
//
