ID G9ZZ37_9PROT Unreviewed; 646 AA.
AC G9ZZ37;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=FAD binding domain protein {ECO:0000313|EMBL:EHM01755.1};
GN ORFNames=HMPREF9946_01822 {ECO:0000313|EMBL:EHM01755.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM01755.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHM01755.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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 PheA/TfdB FAD monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007801}.
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:EHM01755.1}.
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DR EMBL; AGEZ01000060; EHM01755.1; -; Genomic_DNA.
DR AlphaFoldDB; G9ZZ37; -.
DR STRING; 1054213.HMPREF9946_01822; -.
DR PATRIC; fig|1054213.3.peg.1683; -.
DR eggNOG; COG0654; Bacteria.
DR HOGENOM; CLU_009665_9_2_5; -.
DR Proteomes; UP000003292; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02979; PHOX_C; 1.
DR Gene3D; 3.40.30.20; -; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012941; Phe_hydrox_C_dim_dom.
DR InterPro; IPR038220; PHOX_C_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR43004:SF6; FAD_NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR PANTHER; PTHR43004; TRK SYSTEM POTASSIUM UPTAKE PROTEIN; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF07976; Phe_hydrox_dim; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000003292}.
FT DOMAIN 36..410
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 448..612
FT /note="Phenol hydroxylase C-terminal dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07976"
SQ SEQUENCE 646 AA; 71720 MW; 0FB5E245BB082EDA CRC64;
MSMQFHLNGF RAGDPEMSPL DLPAPPAALT PLPATTDVLI VGCGPAGLTL AAQMAAFPGI
TTRIVEQKPG PLMLGQADGI ACRTVEMFNA FGFAERVLRE AYWVNETVFW KPDETRRAAI
RRSDRIQDTE DGLSEFPHVI LNQARVHDFY LESMRRGAAP IEPDYQRRFA GLEVAAPAQA
SSYPVTVRLE RVDPGHEGEI ETIQARYVVG CDGARSAVRR ALGAALHGDS ANQAWGVMDV
LAVTDFPDMR LKAVIHSAHE GNMLIIPREG GYLVRLYIEL DKLAENERVA SRNIDVSHLI
AAAQRILRPY TLEVKEVAWW SVYEIGQRLC DRFDDVPEGQ EATYPPRVFI AGDACHTHSP
KAGQGMNVSM QDAFNLGWKL ASVLREQAAP SLLSTYSTER RAVAEELIAF DRKLASMFSA
PPKDPNDPNS EGVDPAEFQK YFVQQGRFTA GTAMRYAPSL ITGDATHQHL ARGFTIGMRF
HSAPVVRLAD AKPMHIGHTV KADGRWRLFA FAAAENPADE ASRLHALCRF LEQDTASPLL
RYRLAEEDID AVIDFRAIFQ QAHQELDLNA MPSLLRPAKG RHGLIDYEKM FCPDLKNGPD
IFDLRGIDRA QGCVVIVRPD QHIAHILPLD DHAGISRFFD GFMLRR
//
