ID V9VXL0_9RHOB Unreviewed; 816 AA.
AC V9VXL0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:AHD02449.1};
GN ORFNames=METH_19105 {ECO:0000313|EMBL:AHD02449.1};
OS Leisingera methylohalidivorans DSM 14336.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD02449.1, ECO:0000313|Proteomes:UP000018780};
RN [1] {ECO:0000313|EMBL:AHD02449.1, ECO:0000313|Proteomes:UP000018780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD02449.1,
RC ECO:0000313|Proteomes:UP000018780};
RG DOE Joint Genome Institute;
RA Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP006773; AHD02449.1; -; Genomic_DNA.
DR RefSeq; WP_024091952.1; NC_023135.1.
DR AlphaFoldDB; V9VXL0; -.
DR STRING; 999552.METH_19105; -.
DR KEGG; lmd:METH_19105; -.
DR PATRIC; fig|999552.6.peg.3785; -.
DR HOGENOM; CLU_007884_11_0_5; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000018780; Chromosome.
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..370
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 373..427
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 431..701
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 726..808
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 816 AA; 89440 MW; 77BCF64842042066 CRC64;
MSDLPNTARV VIIGGGVIGC SVAYHLAKLG WKDVVLLERK QLTSGTTWHA AGLIGQLRAS
SNMTKLARYS AELYLGLEEE TGVATGLRQV GSVSAALTEE RREELFRNAA MARAFGVPVE
ELSPKEVKER YEHINLDGVT GGVWLPTDGQ ADPANIALAL AKGARQRGAL VKERIKVTGI
SKDGRRVTGV DWVSDDGQSQ GHIEADMVVN CAGMWGHEVG RMAGVNVPLH ACEHFYIVTE
GIAGLGQMPV LRVPDECAYY KEDAGKILLG AFEPNAKPWA MNGIPDSFEF DQLPEDFDHF
EPILEAACNR MPMLAEAGIH TFFNGPESFT PDDAYHLGLA PEMDNFWVAA GFNSIGIQSA
GGAGMALAQW MEDGQKPFDL GDVDISRMHP FQGNKHYLFE RSKETLGLLY ADHFPYRQKA
TARGVRRTPF HHHLLQQGAV MGEIGGWERA NWFANEGQER EYQYSWKRQN WFENSAAEHK
ALRENAGMYD MSSFGKIRVE GPDAEAFLNY ICGANVSVPA GKIVYTQFLN PRGGIEADVT
VTRLSETVYL VVTPAVTRLA DQTWMMRHKG DFNVVLTDVT AGEGVLAVMG PNARKLLQKV
SPNDFSNEVN PFGTAQEIEL GMGLARVHRV TYVGELGWEI YIPAEMSGHA FETLWEAGQD
MGLKLCGMHM MDSCRIEKGF RHFGHDITCE DNVVDAGLGF AVATGKDDFI GKAAVLARKE
TGPKNRMVQF KLTDAEPLLF HNEPILRDGE YVGYLSSGNY GHTLGAAIGM GYVPCEGESA
ADVLGSTYEI DVCGVKVKAE ASLKPMYDPK SERVKA
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