ID A0A418STD5_9RHOB Unreviewed; 956 AA.
AC A0A418STD5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=FAD-dependent oxidoreductase {ECO:0000313|EMBL:RJE84236.1};
GN ORFNames=D3P04_13985 {ECO:0000313|EMBL:RJE84236.1};
OS Paracoccus onubensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1675788 {ECO:0000313|EMBL:RJE84236.1, ECO:0000313|Proteomes:UP000284202};
RN [1] {ECO:0000313|Proteomes:UP000284202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1011MAR3C25 {ECO:0000313|Proteomes:UP000284202};
RA Jurado V., Gutierrez-Patricio S., Gonzalez-Pimentel J.L., Miller A.Z.,
RA Laiz L., Saiz-Jimenez C.;
RT "Acidovorax cavernicola nov. sp. isolated from Gruta de las Maravillas
RT (Aracena, Spain).";
RL Submitted (SEP-2018) 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:RJE84236.1}.
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DR EMBL; QZCG01000009; RJE84236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A418STD5; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000284202; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR042204; 2Fe-2S-bd_N.
DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR028896; GCST/YgfZ/DmdA.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR041117; SoxA_A3.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR Pfam; PF17806; SO_alpha_A3; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000284202}.
FT DOMAIN 485..569
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 580..843
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 867..948
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 956 AA; 103531 MW; 6518AA6CFBC9093B CRC64;
MNRLGNGWGS RIDRSAHIGF TFEGRSMAAH PGDTIASALA ANGEWILSRS FKYHRPRGIL
TMAGQDANTL VQIGDEANAR ADLRPVTEGI SVMPQNVSGS LRRDRGRIID HLGRFLPVGF
YYRSFFGPGR NSWLKWWEPI IRKSAGLGVV NLDPAPRRYL KETRYCDVLV VGAGPAGLAA
AIRAAEAGAD VLLVEKEPDL GGALTYARFD VETADAAEKL AGLGDRAAML PNLTVLPGAT
CNGYFTDHWM PVLYGDRLIR IRASELVLAT GAHEQPLTFR NNDLPGVMLS SAAQRLMRHY
AVRPGQRAVV YACDRDGYLT ALDLDDAGLQ IAAVVDPEVG DRDGLSVELA RRGIRVMRGC
RILQARGNLH LKAVEIQDGK GAGTRLDCDL LVMAGGYTPG YQLALHAGAR LSSDDSGTHF
SITDVPAHIH LAGAVAGLFD LAAVIASGEI AGTRAAAGLG LAVAPDLPPV QTGWRRVTPL
LAHPKGRDFV DFDEDLQVKD IENTVADGYR ELELVKRYST VGMGPSQGRH AALATARIVA
RKTARSLAEI GITTSRPPFG PEKLGLLADT TPERYRHTAL HAAHLAAGAR MMPVGAWWRP
FVYPGQDSVA DAIRREIRMV REAAGMLDVS TLGKLELRGP DAAVFLDRVY TMAHASQPVG
RVRYCLALNE MGSILDDGVA FRLAEDHFYV TATTGAVERL YAEMMLQKTI HGMNVDIQNV
TAAFAAINLT GPRAREVLQR LSGTLDFSRE GFAFLDGRRG ELVGCPVRVM RIGFTGELSY
EIHLPQSHAA GLWAALLEAG ADLGLRPYGL EASRILRLEK GHIIIGQDTD ALTTPDELDM
GWALSRKKPF YMGKAAIERR RRLGEKRCLC GFVLPGENMA EIGESSLVLK EGHPVGHVTS
FGYSPSLAKW IGLAYVAPDQ AGPGAQIRLR GFTGAEIDAE VTALPFYDAE NTRQEM
//