ID I9B1M7_9FIRM Unreviewed; 475 AA.
AC I9B1M7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:EIW19047.1};
GN ORFNames=FB4_0572 {ECO:0000313|EMBL:EIW19047.1};
OS Pelosinus fermentans B4.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW19047.1, ECO:0000313|Proteomes:UP000004324};
RN [1] {ECO:0000313|EMBL:EIW19047.1, ECO:0000313|Proteomes:UP000004324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:EIW19047.1,
RC ECO:0000313|Proteomes:UP000004324};
RX PubMed=22933770; DOI=10.1128/JB.01174-12;
RA Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL J. Bacteriol. 194:5147-5148(2012).
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:EIW19047.1}.
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DR EMBL; AKVJ01000022; EIW19047.1; -; Genomic_DNA.
DR RefSeq; WP_007933619.1; NZ_AKVJ01000022.1.
DR AlphaFoldDB; I9B1M7; -.
DR PATRIC; fig|1149862.3.peg.2003; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000004324; 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; 3.30.70.2190; -; 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; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 42..222
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 475 AA; 51897 MW; FAC6920B0837DB94 CRC64;
MQFNKITENI IKQLEAILGK ANVVVDEEKM EMYSRDETSD KLWEKMPEVV IKPENAQQIA
EVVKLANREL VPITPRGGGS GLAAGAVPLH GGMVLSLEKM NKILEIDKEN LFMVLEPGVT
TGEVQKEAKE LNLFYAGDPC SAESSFIGGN VATNAGGNKA IKYGVTGRHV YGLEVVMPDG
EIVVYGGKNV KDVTFYDMVH LMVGSEGTLG IITKIWLKLM PLPQYVADLL VPFPDMQSAI
KVVPKIMTAG IIPTAVEFMD SLSIKAAELY LNKKLPFSDA GAYIICEVDG NTELQVQEDY
ETIGKLCKEN GALEVFVADN ISTQDRIWKS RKAYAEALRM LSPVYCMEDI VVPIANIPAA
LDAIEKIAAK FECKIPSAGH AGDGNIHATI LREDRDEHAW HDLKDSVLAE IYDAVYALEG
NLSGEHGIGA KRISAMYKHM TEGQKKVLKT VKEAFDPNNI MNPGKVVLLG TIAES
//
