ID A0A127JT96_9BURK Unreviewed; 835 AA.
AC A0A127JT96;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:AMO23160.1};
GN ORFNames=UC35_09975 {ECO:0000313|EMBL:AMO23160.1};
OS Ramlibacter tataouinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO23160.1, ECO:0000313|Proteomes:UP000070433};
RN [1] {ECO:0000313|EMBL:AMO23160.1, ECO:0000313|Proteomes:UP000070433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-10 {ECO:0000313|EMBL:AMO23160.1,
RC ECO:0000313|Proteomes:UP000070433};
RX PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT description of the genus Ramlibacter.";
RL Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP010951; AMO23160.1; -; Genomic_DNA.
DR RefSeq; WP_061498746.1; NZ_CP010951.1.
DR AlphaFoldDB; A0A127JT96; -.
DR PATRIC; fig|94132.3.peg.2029; -.
DR OrthoDB; 9774591at2; -.
DR Proteomes; UP000070433; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000070433}.
FT DOMAIN 9..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 368..422
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 424..727
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 753..829
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT REGION 455..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 835 AA; 90734 MW; A514A9D99330784B CRC64;
MNLPSQAQIV IVGGGIAGCS VAYHLAKLGR TDVLLLEQGK LTSGTTWHAA GLVGQMRPNR
AMTQLSKYGI ELYATLEAET GLATGWKRCG SVNVARTPDR MQVFKKQLAL ARSFGVECHE
ISPREAGEKV PVMRTDDLQG ALWLPGDGKA NPADLCMSLA KGARLRGVKI AEGVEVTGVI
TEHGRVAGVR TSEGEVRCEV LVNCAGQWAR QFGALAGVNV PLFSAEHFYI VTGRIEGVHP
MLPVMRDPDG FIYYKEEVGG LLMGGFEPQA KPWKVDPIPR DFQFQLLDED WDQFEPLMTN
ALHRTPCLAS AEVKLLLNGP ESFTPDGNFI LGEAPELRNY FVCAGFNSAG IANSGGAGRL
MAEWILAGEP GQDVWEVDIR RFAPFTGNRR ALAQRTGETL GLHYAMRWPR QELESARPLR
TSPLYDILAA KGAEFGSKNG WERVNYFRPP LAPSPSGGGL EWGRDGASSE SNTPLPTSRG
EAQFHGRPPH TLGTPGWLPW MLEEQKATRD AVAIYDQTSF AKLLLQGSDA LALLERLCAN
EMDVPVGKMV YTPMLNERGG IESDLTVMRQ AADRFLIVTG SAQATRDADW IGRHIAPGQH
AVLTDVSAMY AVLSVMGPKV RDLLPRVSPD DLSPEALKFS WTREIDVGFA RVRAARMSYV
GGPGYELYVP IEMARHVYLA LADAGAELGL RDAGYYALDA LRIEQGRRAW GAELGPDETP
WEAGLHFSVR PDKATPFIGQ PALRRAQGQP LRKKLVTLLL APPAYAWGGE TILLGGEPAG
EISSAGYSPL AGCCVALGYV RGAAAQVRHE GSEAHIDLWG EAVAVRLHDR WPPAR
//