ID A0A3T0NAC8_9RHOB Unreviewed; 807 AA.
AC A0A3T0NAC8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:AZV80939.1};
GN ORFNames=EBB79_23745 {ECO:0000313|EMBL:AZV80939.1};
OS Parasedimentitalea marina.
OG Plasmid pw43c {ECO:0000313|Proteomes:UP000283063}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Parasedimentitalea.
OX NCBI_TaxID=2483033 {ECO:0000313|EMBL:AZV80939.1, ECO:0000313|Proteomes:UP000283063};
RN [1] {ECO:0000313|EMBL:AZV80939.1, ECO:0000313|Proteomes:UP000283063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W43 {ECO:0000313|EMBL:AZV80939.1,
RC ECO:0000313|Proteomes:UP000283063};
RC PLASMID=pw43c {ECO:0000313|Proteomes:UP000283063};
RA Cao J.;
RT "Parasedimentitalea marina sp. nov., a psychrophilic bacterium isolated
RT from deep seawater of the New Britain Trench.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP033222; AZV80939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3T0NAC8; -.
DR KEGG; sedi:EBB79_23745; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000283063; Plasmid pw43c.
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: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 Plasmid {ECO:0000313|EMBL:AZV80939.1}.
FT DOMAIN 6..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 722..799
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 807 AA; 88213 MW; 24FD2EF14931B4AC CRC64;
METSARVVII GGGVVGCSIL YHLAKRGWKD VVLLERQELT AGSSWHAAGN LFTLTAPGNA
AILQKYTIDL YPELEKESGQ DCGLHYNSEL LVAKDEEEIK TLSIAHAFGK RYGIESEFIS
AEQAKKLAPT LNTDDLTAIL HEKSAGYCDP SSVTHAFAKA ARNYGASIHR HTPVLETNQR
HDGKWDVVTE NGTITTDYVV NAAGLWGREV AALAGITLPL MPVEHHYLVT EEVPEMANLE
TPHALLSYAD ANLYMRPEGK GLLIGAYESK CVHWAEDGTP LEFGHELLPD DLSRMEDEFL
QAVELMPCLA EAGIKSVING PMIFSPDLGP LIGPYPGKPG YICANGVMTG FNQGGGIGKV
LAEWIIDGEP SLDVSFWDVA RYGDYADSHY TKEMTKYWYE NRSSRVYPYQ TFPAARPMKM
SPIHDRLKEA GAVFGETCGW EDAYWYPKND AERVEEYSYE RPAWFAAVAR ESRAVRETAG
LFELTSYGKY MFSGAGAVAF LDRILANKIP ELIGKTALCP MLSEMGKVIG DFTVTRLGPE
RCLVLGSGSM EKIHERWFLA QLPDAGVSYD NLTNSYAGLH VAGPNARAIL QTLAPGTSFE
SADFPFLSGR EMALGSCPDA LVVRVSYTGE CGYEIYMPLE HQAALYDKII EAGEPHGLTL
AGGHALMALR LEKGFAGWGM ELTSDYYPNE TALARFVRYG KGDFIGRKAA LAAKEAGPRE
SFVQFAVDTK EADPYGGEPV FKDGELVGYT SSGGFGYCAG TSLALGYLQP ESIDPDAVYQ
VDIVGKKCNA RLLSAPPVDP EGLRMRR
//