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Database: UniProt
Entry: A0A0U4VI61_9GAMM
LinkDB: A0A0U4VI61_9GAMM
Original site: A0A0U4VI61_9GAMM 
ID   A0A0U4VI61_9GAMM        Unreviewed;      1013 AA.
AC   A0A0U4VI61;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-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=ATY27_14440 {ECO:0000313|EMBL:ALZ76838.1};
OS   Rheinheimera sp. F8.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=1763998 {ECO:0000313|EMBL:ALZ76838.1, ECO:0000313|Proteomes:UP000059499};
RN   [1] {ECO:0000313|Proteomes:UP000059499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8 {ECO:0000313|Proteomes:UP000059499};
RA   Schuster A.K., Szewzyk U.;
RT   "Draft genome sequence of Rheinheimera sp. F8, a biofilm-forming strain
RT   which produces large amounts of extracellular DNA.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALZ76838.1, ECO:0000313|Proteomes:UP000059499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F8 {ECO:0000313|EMBL:ALZ76838.1,
RC   ECO:0000313|Proteomes:UP000059499};
RX   PubMed=26966195;
RA   Schuster A.K., Szewzyk U.;
RT   "Draft Genome Sequence of Rheinheimera sp. F8, a Biofilm-Forming Strain
RT   Which Produces Large Amounts of Extracellular DNA.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP013656; ALZ76838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U4VI61; -.
DR   Proteomes; UP000059499; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059499}.
FT   DOMAIN          48..281
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1013 AA;  111422 MW;  3818296C9CB97E4E CRC64;
     MIPKLNPEQM LAPVVVQYCA SLQQAGFQGE IETSYASRLA VATDNSVYQA LPQAVLLPKH
     QQDVELLTRL ASEPRFSALK FAPRGGGTGT NGQALTEHLV VDLSRHLRTI LDFDPQKRQV
     RVQAGVIKDQ LNAYLAPFGF FFAPDLSTSN RATIGGMINT DASGQGSLVY GKTSDHVLAL
     TTVLADGTVL KTAPQPLGEA EVKASLDNAE GHIYRQVLAS CRQFRPQILA KFPRLNRFLT
     GYDLEHVFNA DLTEFDLGRV ITGSEGSLGF VTEALLNVTP IARHKCLVNV KYNSFESALR
     NAPFLVAANA TSVETVDSKV LNLARQDIIW HQVKTYIEDV PGQDMLGLNM VEFNDEDDAG
     MAQKVAHLEE RLQHALDNGD SGIIGYQLTY DPKAILQIYA MRKKAVGLLG NAKGSQKPVP
     FTEDTAVPPE NLADFIMEFR ALLDSHGLSY GMFGHVDAGV LHVRPALDLC EPGQETLLRT
     ISDQVVALTA KYGGLMWGEH GKGYRSEYGP AFFGEELFAE LRKIKGVFDP LNRMNPGKIC
     TPWQSQDELV SVDGQKRAYF DRQIPTVVRQ SFEAATSCNG NGLCFNYEEN SPMCPSSKIT
     KDRRHSPKGR AGLMREWLRL MQKQGVDVLA QEQQLLQASS GPAALLQKVQ NTVGKWRGEA
     DFSHEVMEAM EGCLACKACA GQCPIKVDVP SFRARFIQLY HSRYLRPLKD YIVGNIERSA
     PVLAKAPGLV NAVVTLPPVA WLLKKVVGYV DTPLLSTPVL TERAAQYRAF DLAALQALPA
     TEKAKLVLLV QDPFTSFYEA DLVADAMALL RKLGFDPVLL PFLPNGKPQH VKGFLREFAE
     TARTASEFLQ QVSTLGAPML GLDASLVLVY RDEYVKALGE ARGDYQVQLL HEWLQLQQLP
     ALHNSGQFKL LAHCTEKTAL PATEKSWQQI YQQAGLSLQV VATGCCGMAG TYGHEAQNEA
     NSKALFNLSW AAPVQQTAPD LLLVTGFSCR SQVKRYEGFK PKHPLQALLQ LMP
//
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