ID G8PTP5_PSEUV Unreviewed; 1000 AA.
AC G8PTP5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Sarcosine oxidase, alpha subunit family protein {ECO:0000313|EMBL:AEV37466.1};
GN OrderedLocusNames=PSE_2958 {ECO:0000313|EMBL:AEV37466.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV37466.1, 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};
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:AEV37466.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV37466.1,
RC 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; CP003147; AEV37466.1; -; Genomic_DNA.
DR RefSeq; WP_014285532.1; NC_016642.1.
DR AlphaFoldDB; G8PTP5; -.
DR STRING; 911045.PSE_2958; -.
DR KEGG; psf:PSE_2958; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_011963_0_0_5; -.
DR Proteomes; UP000005634; Chromosome.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:InterPro.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:InterPro.
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; 1.
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; IPR023753; FAD/NAD-binding_dom.
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; IPR006277; Sarcosine_oxidase_asu.
DR InterPro; IPR041117; SoxA_A3.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR NCBIfam; TIGR01372; soxA; 1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF17806; SO_alpha_A3; 1.
DR PIRSF; PIRSF037980; SoxA; 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}.
FT DOMAIN 173..443
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 518..601
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 618..882
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 907..992
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 1000 AA; 108994 MW; 14FD8B7DC898838E CRC64;
MSNLRVDGKG RINRDKRIRF TFDGVSYEGF EGDTVASALL ANGVHLMGRS FKYHRPRGPV
TAGSEEPNAL IGTSRGGAGR FEPNTRATVQ EIYEGLTTVS QNKWPSLNFD VGAINDKLHK
LFAAGFYYKT FMWPKSFWDK VYEPVIRASA GLGVSPSEPD ADTYASRYLY AELLIVGAGP
AGLAAALTAA RNGTDVVLVD ENRELGGSLL SEAPASIDGK PAEAWLSECI EELKACPNVR
IMTRSVAIGY YHENMVGVAE KLTDHLAYPP AGAPRERMWR IRAKEVILAQ GALERPLVFD
GNDRPGVMMA SAAQTYLNRY GVKVGTAAVV MTSHDSAWYA AFDLADAGVT IAALVDVRSS
VGDHLLSEAR ARGITVKTGH TVTSVAGKKR VSGTQVGRVT GDGKVADITQ VSCDIVLMSG
GWTPSLHLFS HTKGSLHWDE ENEVFLPGEK TERCHIAGGG RGLWSQQAAF DDGVHAAEQA
LVSLGQTAKT ISVDVDGDRA GSGIVMEELP SNDDKLARRA FVDFQNDVTA KDIRLAVREG
MLSIEHVKRF TTNGMATDQG KMSNMNGLKI AADELGRPAP KVGLTTFRPP YTPTTFGTFA
GYHKDELFEV TRKTNIDSWA EENGAVFEPV SLWRRAWYYP KAGEDLHAAV ARECRETRAS
VGMFDASTLG KIEVVGPDAA EFMNRMYTNP WTKLAPGRCR YGLLLGEDGF IRDDGVIGRI
SQDRFHVTTT TGGAARVLTM MEHFLQTEWP DLDVWLTSTT EQWSTIALNG PNARKVLEPF
VKGTDLSAEA FPHMALRECT VGGFEARLFR VSFTGELGFE VNVPSEHGRA LWEMLYQEGK
KYDMCVYGTE TMHVLRAEKG YIIVGQDTDG TVTPADAGLT WAIGKKKPDF VGKRSLTRPD
MLLANRKQLV GLLTEDPSVV LEEGAQIVES GDTSIPAKML GHVTSSYWSE ALGRSIAMAL
IEGGFERDGK SIDVPMPGQT HRATVTGTVF YDPDGERINL
//
