ID A0A0T5ZJW2_9CHLR Unreviewed; 814 AA.
AC A0A0T5ZJW2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:KRT63090.1};
GN ORFNames=XU10_C0015G0011 {ECO:0000313|EMBL:KRT63090.1};
OS Chloroflexi bacterium CSP1-4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT63090.1, ECO:0000313|Proteomes:UP000051896};
RN [1] {ECO:0000313|EMBL:KRT63090.1, ECO:0000313|Proteomes:UP000051896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT63090.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT63090.1}.
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DR EMBL; LDXM01000015; KRT63090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZJW2; -.
DR STRING; 1640513.XU10_C0015G0011; -.
DR PATRIC; fig|1640513.3.peg.1461; -.
DR Proteomes; UP000051896; 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 9..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 367..421
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 424..695
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 721..806
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 814 AA; 89714 MW; 63D4BE2BA45FD9F9 CRC64;
MTLPSHAQAV VIGGGIVGCS VAYHLTKRGW RDVVLLERKQ LTSGTTWHAA GLVTQLRATY
NMSMLAKYSA ELFPELERLT GLGTGFRRTG SILLATTDER WTEVRRQISM ARVCGFEVQP
ISPAEAAAMW PLLDPSGVVG AVFLPGDGIA NPTDVTQALA AAARLGGARI LEHTAVTGVL
RRDGRVTGVS TAQGDIASEI VVNCTGMWAR ELAARSGVTV PLHAAEHFYV ITEPVPGLSR
DLPVLRSPDD TAYLREDAGK LMVGFFEPGA KPWATHGIPD DAAFVTLPED WDHLAPYLEM
AARRVPLLRD IGIQLFFNGP ESFTPDDRYI LGEAPGLRGY FVAAGFNSVG FQSGGGAGRA
VADWVVDGHP PMDLWEVDIR RFMPFQGNRR YLRERTTETL GLLYDMHWPF RQVETARGVR
RTPFHDRLAA RGACFGEVAG WERANWYAPA GVEPRYEYSY GRQNWFPFSA EEHRAVRGGV
GLFDQTSFGK ILVQGRDAER TLNALCTADV AVEPGRIVYT QWLNERGGIE SDVTVTRLDE
RSFLVVTTGT SLVRDLDWLQ RGIPDEAHAF VTDVTHAFAV LSVMGPRSRE LLAALTDADL
SNEAFPFATS REIDLGYALV RASRITYVGE LGWELYVPTD VATHVYDTIV AAGERVGLRH
AGYHALNSLR IEKAYRHWGH DMTDEDTLLE AGLAFTAAWD KPGGFIGREA LLRQRERGLA
RRLAIFALED PEPLLYHNEP IWRDGRLVGR ISSGMYGHTL GRSIGLGYVR NDAGPATAEW
IAAASYELEI ATERFPATVS LRPPYDPGNE RIRS
//