ID C3MIT3_SINFN Unreviewed; 997 AA.
AC C3MIT3;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Sarcosine oxidase, alpha subunit {ECO:0000313|EMBL:ACP26646.1};
DE EC=1.5.3.1 {ECO:0000313|EMBL:ACP26646.1};
GN Name=soxA1 {ECO:0000313|EMBL:ACP26646.1};
GN OrderedLocusNames=NGR_c29020 {ECO:0000313|EMBL:ACP26646.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP26646.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP26646.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CP001389; ACP26646.1; -; Genomic_DNA.
DR RefSeq; WP_012709401.1; NC_012587.1.
DR RefSeq; YP_002827399.1; NC_012587.1.
DR AlphaFoldDB; C3MIT3; -.
DR STRING; 394.NGR_c29020; -.
DR KEGG; rhi:NGR_c29020; -.
DR PATRIC; fig|394.7.peg.5740; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_011963_0_0_5; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000001054; Chromosome.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-EC.
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,
KW ECO:0000313|EMBL:ACP26646.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT DOMAIN 172..434
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 516..596
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 613..879
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 904..989
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 997 AA; 107679 MW; 46715B5C55C07807 CRC64;
MSGVNRISGA GRLTPARTAR FTFDGRTLTA LEGDTVASAL IANDIHLVGR SFKYHRPRGI
LSAGAEEPNA LLDVSRDAAR RQPNVRATVQ EVFDGMKVSS QNRWPSLAFD VGGFNDLLSP
FFAAGFYYKT FMWPKAAWHS LYEPFIRRAA GLGVAPTEPD PDHYASRYVH CDVLVVGAGV
AGLAAALAAA KAGAKVFLCD EQPEVGGALH HDTGTVVDGK PGYVWAQETG KALAGMDNVT
VLTRTTAFGY YNHNFVGLVE RVTDHLAAVD KALPRERLWQ VRAKKVILAN GAIERHMVFA
NNDRPGIMLA SAGRTYLNHF GVAVGKKVGI YTAHDSAYEA AFDLRKAGVA VAAIVDCREQ
PGEAVLEKAR HLGIEVLTGH SVVNTTGKLR IASITVARNG GRGARKIPVD ALLVSAGWTP
SVHLFSQSRG KVKFDAETER FLPGTYAQDC LSIGTCNGTD DLQATIDEAL AAGELAARAA
GAEGGEQVAL TGQNAFEWTG GMIGAAEGAG PDTTVKAFID FQHDVCAKDI RLAVREGMHS
VEHIKRFTTN GMASDQGKLS NMHGLAIAAE ALGKGIPEVG LTTFRQPYTP ITFGTIVNHS
RGSLFDPARK TPMHAWEEAQ GAEFEDVGNW KRAWFYPKAG EDMHEAVARE CKTVREVAGV
FDASTLGKIE VVGPDAAQFL NLMYTNAWDN LKPGRCRYGI MLRDDGFVYD DGVVGRLAED
RFHVTTTTGG APRVLHHMED YLQTEFPHLK VWLTSTTEQW AVIAVQGPKA REIIAPLVEG
IDLSNEAFPH MSVAEGRICG VPTRLFRMSF TGELGFEVNV PADYGQAVWE AIWARAEPMG
ACAYGTETMH VLRAEKGYII VGQDTDGTLT PHDAALSWAV SKKKPDFVGI RGLKRPDLVK
DGRKQLVGLL TKDPKVVLEE GAQIVADPNE PKPMTMLGHV TSSYWSSNCG RSIAMAVVAG
GQARLGQTLY VPMADRTIAV EVSDMVFFDK EGGRLHG
//
