ID A0A0X3TL18_9RHOB Unreviewed; 805 AA.
AC A0A0X3TL18;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KUJ76487.1};
GN ORFNames=AVO45_11905 {ECO:0000313|EMBL:KUJ76487.1};
OS Ruegeria marisrubri.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ76487.1, ECO:0000313|Proteomes:UP000053791};
RN [1] {ECO:0000313|EMBL:KUJ76487.1, ECO:0000313|Proteomes:UP000053791}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ76487.1,
RC ECO:0000313|Proteomes:UP000053791};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-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:KUJ76487.1}.
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DR EMBL; LQBQ01000035; KUJ76487.1; -; Genomic_DNA.
DR RefSeq; WP_068348373.1; NZ_LQBQ01000035.1.
DR AlphaFoldDB; A0A0X3TL18; -.
DR STRING; 1685379.AVO45_11905; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000053791; 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:SF187; DIMETHYLGLYCINE DEHYDROGENASE, 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053791}.
FT DOMAIN 7..364
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 367..420
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 424..691
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 721..797
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 805 AA; 89281 MW; E17A14EEE8918C47 CRC64;
MKSHAQAVVI GGGLAGCSIL YHLAKLGWTD VILLERDELT SGSTWHAAAN IHGLHDNNNV
TRIQHYTMNL YKELEKETGQ GCGVFQPGSL YLAQTEAREH QLRLQEAKAR FYGLNFHEIS
REQAMELHPL AQFDDVRCIM YEPDGGNVDP SGVTHAYAAG ARALGAEIRR FCPVIGTEAQ
PDGSWIVRTK KGDIHTQWVV NAAGLWGREV AALAGLELPL QPTEHQYFVT EAIDEVAALG
RRLPSIADRD GEYYFRQEGN GLLIGAYEKD MRFWAEDGTP LDFAHDLFPD DLDRIMENVI
RATERVPVAA TAGVKRVING PMIWSPDSNA IWGPVPELRN YFCCTGIIPG FSQSGGLGLL
AAQWMIEGEP QYDMFAWDLA RFGDWADKKF TKARVADQYS HRFAIHFPNE ERSAGRPARV
RPAYEMQKQM GAVFGLNCGW EHPLWFADQP GTFETIGFTR QNWFEPVGQE ARMLRESVGV
IDISNFANYV IKGPGAHDWL DRLVANRVPT QVGRSCLTPL ISVRGGVAGD FTITKTAQDE
YMMIGSGMAE RYHQRFFNMV ELPEGTTFEV ATNRIAGFNV AGPKSREMLQ RLTNMDLSNA
AFRFMRSATI EVAGVTCLAI RVSFTGDLGW ELHCAEEDQT RLYAGLLDAA RKFNGGPVGS
RALGALRIEK GYGSWGREYS QEYWPQEVGL TGLIKLDKDF LHKDAYLSVR DNTPREALSI
FEVEAIHDAD ASGGEPIFAP DGTPVGRVTS GAYGYSVGKS LALGFRNPQV ARPGDEVEVF
ILGKPHKARV LEQPPFDPQG ARLRG
//