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Database: UniProt
Entry: F7Y7V9_MESOW
LinkDB: F7Y7V9_MESOW
Original site: F7Y7V9_MESOW 
ID   F7Y7V9_MESOW            Unreviewed;       997 AA.
AC   F7Y7V9;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Sarcosine oxidase, alpha subunit family {ECO:0000313|EMBL:AEH86341.1};
GN   OrderedLocusNames=Mesop_1860 {ECO:0000313|EMBL:AEH86341.1};
OS   Mesorhizobium opportunistum (strain LMG 24607 / HAMBI 3007 / WSM2075).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=536019 {ECO:0000313|EMBL:AEH86341.1, ECO:0000313|Proteomes:UP000001623};
RN   [1] {ECO:0000313|EMBL:AEH86341.1, ECO:0000313|Proteomes:UP000001623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24607 / HAMBI 3007 / WSM2075
RC   {ECO:0000313|Proteomes:UP000001623};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Misra M., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Mavrommatis K.M., Tiwari R.P.,
RA   Howieson J.G., O'Hara G.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium opportunistum WSM2075.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; CP002279; AEH86341.1; -; Genomic_DNA.
DR   RefSeq; WP_013893067.1; NC_015675.1.
DR   AlphaFoldDB; F7Y7V9; -.
DR   STRING; 536019.Mesop_1860; -.
DR   KEGG; mop:Mesop_1860; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_011963_0_0_5; -.
DR   Proteomes; UP000001623; 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}.
FT   DOMAIN          172..451
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          614..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;  107141 MW;  227AEECD91D8E34F CRC64;
     MSGGFRIPSA GRLSQAKTAR FSFDGQPYTG IEGDTLASAL LANGVHLVGR SFKYHRPRGI
     LSAGAEEPNA LVQIVRDDAR KTPNVRATVQ ELYDGLAANS QNRWPSLSFD IGAVNDIASP
     MFSAGFYYKT FMWPKAAWKS FYEPKIREAA GLGVSPDKPD PDHYSSRYAH CDVLVLGGGA
     AGIAAALAAA ETGVRVILAD EQVEFGGSLR FESGAKIDGQ DGFAWAQAAI ARLSAMDNVR
     VLSRTTAFGY YAQNFVGLVE RVSDHLKAPG HDLPRERLWQ VRAKRVVLAS GAIERHMVFA
     NNDRPGIMLA GAARTFLNHY GVAVGRNVGV YTANDSAYAA AIDLKKAGVN VAAIVDLRDN
     PTGPVIDEAR ALGIEINFGR AVIRAGGKLR VSSMTVQPKN GGGERTIPVD AILMSAGWTP
     SVHLFSQSRG KVAFNDETKR FVPGIYAQDC VSVGACNGTD GLSATVDEAY AAGAKAAKDA
     GAKTAKGAKP KVDASESWSR GMLGAGPGAG PDTTVKAFVD FQNDVTAKDI RQAVHEGMRS
     IEHVKRFTTN GMATDQGKTS NMHGLAIAAE TLGKPIPEVG LTTFRAPYTP VTFGAIVSHA
     RGPLFDPTRK TAIHPWAEAQ GAVFEDVGQW KRAWYFPKAG EDMHAAVDRE CVAVRNKAGL
     FDASTLGKIE VVGPDAAKFM ELLYTNPWEK LEPGRCRYGI MLREDGFIYD DGVVGRLAPD
     RFHVTTTTGG APRVMNHMED YLQTEFPHLN VWLTSITEQW AVIAVQGPKS RDIIAPLVEG
     IDMSDEALPH MSVREGKICG VPTRLFRMSF TGERGFEVNV PADYGQAVWE ALWAEGQKHG
     AAAYGTEAMH VLRAEKGYII VGQDTDGTVT PGDAGLDWAV GKKKADFVGI RGLTRPDLVA
     KGRKQLVGLK TKDPKVVLEE GAQIVEDPKQ AIPMKMIGHV TSSYWSENCG RSIALALVAG
     GRDRMGDTLY VPMPNGVIEV EVTGMVFFDE TGGRLNG
//
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