ID G8PV23_PSEUV Unreviewed; 831 AA.
AC G8PV23;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Aminomethyl transferase family protein {ECO:0000313|EMBL:AEV39611.1};
GN OrderedLocusNames=PSE_p0029 {ECO:0000313|EMBL:AEV39611.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OG Plasmid FO-BEG1 {ECO:0000313|Proteomes:UP000005634}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV39611.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RC PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV39611.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV39611.1,
RC ECO:0000313|Proteomes:UP000005634};
RC PLASMID=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP003148; AEV39611.1; -; Genomic_DNA.
DR RefSeq; WP_014290151.1; NC_016646.1.
DR AlphaFoldDB; G8PV23; -.
DR KEGG; psf:PSE_p0029; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_11_1_5; -.
DR Proteomes; UP000005634; Plasmid FO-BEG1.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase 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.
PE 3: Inferred from homology;
KW Plasmid {ECO:0000313|EMBL:AEV39611.1};
KW Transferase {ECO:0000313|EMBL:AEV39611.1}.
FT DOMAIN 8..376
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 379..433
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 437..699
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 725..798
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT REGION 797..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 92563 MW; C1FBBF6704A69DF6 CRC64;
MSIPDTARVV IIGGGVVGVS TLYHLAKMGW SDCVLLEKNE LTAGSTWHAA GNCPNFATSY
AVMNMQRYGL ELYRGLAEEV NYPINYHVTG AIRLAHSHER MMEFEHVAAM AEHMGLSMDM
CTPDQLQEHF PFMEVHDLEG GLWDPLDGDI DPAQVTQALA KGARDLGARI LRFTPATGVR
REGGEWIVCT EAGEIRCEYV VNAAGYYAAR VGEWFEPYGG RSVPTITMSH QYFMTEAIPE
VEAWTKQHGR KLPMLRDPDT SYYLRQETGG FNLGPYERAC RTAWTTPDDP MPEDFSFQLY
PDDLERLEFY IEDAMARVPL LGTQGVKRNI NGPIPYAPDG LPMIGPMPGV PNAFEAHSFT
FGIAQGGGAG KVAAEWIVNG QTEWDMWAVD PRRYTDYTDK QYCIDKAKEV YGHEYAMHFP
HHEWPAGRDR KLSPNHTKLL ELGGQMGAYN GWERANWFAK AGDDTSEEAT QTWARSGPWE
QRVREECEAV RDYVGVLDLP GFSRFKLSGE GAAEWLREQI AGALPKVGRM TLGYFPDERG
RVLTEMSILR HGADEFTLIT AALAQWHDFE LLNARLPEGL LLEDQTRDVT TLIVTGPQSR
QLLAGMTEAD LSLSWLSLQQ AMVLGKQALL VRVSFAGELG WEIHASNEDM PEIYEALLGS
GAKPFGMYAL NTLRLEKGYR SWKGDLSTDY TLFEAGLDRF VKLNKPQNFP GKATLLKEAA
DGVKRRFVTM IVEAGDCDAQ YMSTIWQGDQ MVGEVTSGGW GYRINASIAL GVVHADLGEP
GTELTIKIYG KPHKAVVQPD GPLWDPENVR LRDQGEGKDA DPDQSTSLQT V
//
