ID A0A1F8KJN0_9CHLR Unreviewed; 811 AA.
AC A0A1F8KJN0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=FAD-dependent oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A2X25_04110 {ECO:0000313|EMBL:OGN73926.1};
OS Chloroflexi bacterium GWB2_49_20.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797612 {ECO:0000313|EMBL:OGN73926.1, ECO:0000313|Proteomes:UP000178842};
RN [1] {ECO:0000313|EMBL:OGN73926.1, ECO:0000313|Proteomes:UP000178842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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:OGN73926.1}.
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DR EMBL; MGMF01000017; OGN73926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8KJN0; -.
DR STRING; 1797612.A2X25_04110; -.
DR Proteomes; UP000178842; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 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; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR13847:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 10..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 367..422
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 425..699
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 724..804
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 811 AA; 90497 MW; 8DC018F3D19E0BBA CRC64;
MSEFPTQAQI VVIGGGVGGC SIAYHLAELG WKDVVLLEKH ELTSGSTWHS AGLVGQLRSD
ANLTRMMSYS TDLYRRLKAE TGQDTGWREV GGIRLASSTE RMEDLKRLVG MARSFGVPIE
MISPKEALDM FPLMNMDGIL GAAFTPNDGM IDPTGLTMAL AKGAKMRGVK FFEDTEVTAI
HVEQGRVNEV VTNRGSIKTE IIVNATGQWG GEVSRLVGLN IPVVPMAHLY IITKPIEGVT
SNFPTLRDPD LLVYWREEVG GLITGGYERN PVPFGLNGIP HDFKYQLLPP DWDRFTPLME
NSIKRVPAVE HAEIIQLLNG PEGFTPDGEF LLGPTPVKGF WIACAFCAHG LAGAGGIGKT
MAEWITHGMP EWDVWRLDVR RFGSNYASQD YTVKRTIETY SKYYDIHYPS GERISSRNLR
LSPTYYRLRD LRASFGEKSG WERPNWFSCY EEKANHGHEP KGWYKRNWSR AIGYEHIQTR
EKAGLFDETS FNKFEVRGPD ALKFLNYVCA NEIDVPVGTV VYTECLNKRG GIECDFTVTR
LSEERFFIIT GTAFGLHDLS WLQLNNPEDG SVTIEDVSSS YACIGLWGPK ARNILAKVTR
NDITNDKFPY MTAQHITVGD VPTLAMRVTY VGELGWEMYV PMEYGLRLWD TLWEAGQPEG
LVAAGYRAID SLRLEKGYRY WSGEISPDYT PFEAGLGFAV ELTKTDFIGR EALLKQKEAG
IKIKLCCLSL ADTRSVVLGN EPLRLAGSND IIGWVTSGGY GYTVAKSIAY GYLPVEHATP
GTKLTVECFG EEIEAIIEKE PLYDPKGKRI K
//
