ID A0A0B4BRE4_9RHOB Unreviewed; 805 AA.
AC A0A0B4BRE4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KIC21433.1};
GN ORFNames=RA20_04695 {ECO:0000313|EMBL:KIC21433.1};
OS Leisingera sp. ANG-Vp.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1577896 {ECO:0000313|EMBL:KIC21433.1, ECO:0000313|Proteomes:UP000031177};
RN [1] {ECO:0000313|Proteomes:UP000031177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG-Vp {ECO:0000313|Proteomes:UP000031177};
RX PubMed=25755651; DOI=10.3389/fmicb.2015.00123;
RA Collins A.J., Fullmer M.S., Gogarten J.P., Nyholm S.V.;
RT "Comparative genomics of Roseobacter clade bacteria isolated from the
RT accessory nidamental gland of Euprymna scolopes.";
RL Front. Microbiol. 6:123-123(2015).
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:KIC21433.1}.
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DR EMBL; JWLD01000009; KIC21433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B4BRE4; -.
DR STRING; 1577896.RA20_04695; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000031177; 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;
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 718..797
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 805 AA; 89165 MW; 7612B24CE0005DE2 CRC64;
MKTHAQAVVI GGGLVGCSIL YHLAKLGWTD VVLLERDELT AGSTWHAAAN IHGLHDNNNV
TRVQHYTMNL YKELEKETGQ GCGVFQPGSL YLAKTEEREH QLRLQEAKAK YYGLNFHEVS
REQAKELHPL AQFDDIRCIM YEPDGGNVDP SGVTMAYAAG ARAMGAEVER FCPVIGTEQQ
PDGSWIVKTE KGDIHTQWVV NAGGLWGREV AAMAGLTLPL QPTEHQYFVT ETIDEVANLG
RRLPSIADRD GEYYFRQEGN GFLIGAYEKD MRFWAEEGTP WDFAHELFPD DLDRIMENVI
RATERVPCAE TAGVKRVING PMIWSPDSNA IWGPVPELKN YFCCTGIIPG FSQSGGLGLL
AAQWMIEGEP QYDMFAWDLA RFGDWADKKF TKARVEDQYA HRFAIHFPNE ERSAGRPARV
RPAYEMQKEM GCVFGLNCGW EHPLWFSGTP GTTDTNSFTR QNWWEPVGRE VNMLRENVGV
IDISNFANYV IKGPGAYDWL DKLVANKVPT EVGRSCLTPL ISVRGGVAGD FTITKVADDE
YMMVGSGMAE RYHQRFFNMV ELPEGTTFEV ATNRIAGFNV AGPKSRDMLQ RMTNADLSNE
GFRFMRSRTI DVAGVECLAI RVSFTGDLGW ELHCAEEDQV KLYSALLAAA AEFDGGPVGG
RALGSLRIEK GYGSWGREYS QEYWPQEVGL AGLVKLDKDF LNKEAYLKVK DKAPREVLVG
FEIDAVNNAD ASGGEPVFTP GGEPVGRVTS GAYGYSVGKS LALGYANPET AKPGDEVEVY
ILGKPHTARI LETAAFDPSG ARLRA
//
