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Database: UniProt
Entry: A0A495RUK7_SPHMI
LinkDB: A0A495RUK7_SPHMI
Original site: A0A495RUK7_SPHMI 
ID   A0A495RUK7_SPHMI        Unreviewed;       992 AA.
AC   A0A495RUK7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Sarcosine oxidase subunit alpha {ECO:0000313|EMBL:RKS91227.1};
GN   ORFNames=DFR51_0783 {ECO:0000313|EMBL:RKS91227.1};
OS   Sphingosinicella microcystinivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingosinicellaceae; Sphingosinicella.
OX   NCBI_TaxID=335406 {ECO:0000313|EMBL:RKS91227.1, ECO:0000313|Proteomes:UP000276029};
RN   [1] {ECO:0000313|EMBL:RKS91227.1, ECO:0000313|Proteomes:UP000276029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19791 {ECO:0000313|EMBL:RKS91227.1,
RC   ECO:0000313|Proteomes:UP000276029};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (OCT-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:RKS91227.1}.
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DR   EMBL; RBWX01000007; RKS91227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495RUK7; -.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000276029; Unassembled WGS sequence.
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..432
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          514..596
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          612..877
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          902..984
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   992 AA;  106115 MW;  E53BB69D03CFE552 CRC64;
     MTSSFRTASG GRVDRDRPVN FTFDGKAYVG LHGDTLASAL LANGVHLVGR SFKYHRPRGI
     VGSGADEPNA LVGVRRDAAR YTPNLLATQV ELYDGLAAVS QNRYPSLEYD CMAVNDTLLG
     RFIPAGFYYK TFMWPKGAWD KLYEPRIRKA AGLGVAPTAP DPDVYTQRYA HADILVIGAG
     PAGIAAAQQA AASGARVILA DDRPAMGGSL LAAADTTVDG EDARAWLRGS LAALAALSNV
     TMLPRTIAFG YYPHNWIGLA EKLTDHLPYP ASGQPRERLW QVRARQVVIA AGSIERPLVF
     PDNDRPGIML ADAARTYLQE YGVMVGRKAV IVAAHDSAYR VAHELRAAGI EIAAIVDIRS
     PVPAAQSARD AGLRVLCDAK VEGTRGRLRV SAITITADGK RETLACDTVL MAGGFTPSVH
     LFSQSRGKLV WDEAIQAYLP GESGEAERSA GACRGRFALS EALADGAEAG RSAARDAGFS
     PMDLPIPSAQ GARACGGGGH IGAVPTGADL SRAKAFVDWQ NDVTARDIAL AAREGFLSIE
     HVKRYTTTGM ATDQGKLSNI NALGIVSNVT GRSIPEIGLT TFRAPYTPVT FGTLAGKARG
     DLFDPMRVTA IHDWAAEHGA VFEDVGNWKR ARYFPRHGED MHAAVGRECL QVRNQVGIFD
     ASTLGKIEVV GPDAAEFMNR FYVNAWLKLG VGRCRYGVLL REDGFVLDDG VVGRLAPDRF
     HVTTTTGGAA RVLAMMEDYL QTEWSDLKVW LTSTTEQWSV IAVQGPKARA VLAPLVTGID
     LSAEAFPHMS IADAQICGVP MRLMRVSFTG ELGFEVNVPS GHGRMVWEAI WECGRSNGML
     AYGTETMHVL RAEKGFIIIG QETDGTVTPD DAGLGWAIGK AKPDFVGKRS LARPAMIAPD
     RKQLVGLLTH DAATVLEEGA QITDPLDPRA AIGHVTSAYH SVALGRSIAL ALVRGGRARM
     GHTLHVPMPD GAITAEVVQP VFLDPEGARI HV
//
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