ID A0A1W6CWU3_9RHOB Unreviewed; 976 AA.
AC A0A1W6CWU3;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Sarcosine oxidase subunit alpha {ECO:0000313|EMBL:ARJ69348.1};
GN ORFNames=B0A89_06605 {ECO:0000313|EMBL:ARJ69348.1};
OS Paracoccus contaminans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1945662 {ECO:0000313|EMBL:ARJ69348.1, ECO:0000313|Proteomes:UP000193017};
RN [1] {ECO:0000313|EMBL:ARJ69348.1, ECO:0000313|Proteomes:UP000193017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RKI 16-01929T\LMG 29738T\CCM 8701T\CIP 111112T
RC {ECO:0000313|Proteomes:UP000193017};
RA Aurass P., Karste S., Trost E., Glaeser S.P., Kaempfer P., Flieger A.;
RT "Genome sequence of Paracoccus contaminans isolated from a water
RT microcosm.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP020612; ARJ69348.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6CWU3; -.
DR STRING; 1945662.B0A89_06605; -.
DR KEGG; pcon:B0A89_06605; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000193017; 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; 2.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000193017}.
FT DOMAIN 175..422
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 496..579
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 594..858
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 884..968
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 976 AA; 105991 MW; 914110E11646F3CC CRC64;
MTTRNPPFRL PAGGRLIDRA ARRDFRFDGR PLSGLAGDTL ASALLASGQL MMGRSFKYHR
PRGPIASGAE EPNALLGLGQ AGRFEPNQRA TTTPLVQGMV TTSQNAWPSL ERDIGAINDA
LWRFFPAGFY YKTFIHPRAA WKHLFEPVIR RAAGLGRAPD QRDPDRYEQA YDFVDVAVVG
GGIAGLTAAA EIGAAGRRVL VLEQNGHWGG RTPVDHPDGQ ARVDELLSRL RDMANVTLRR
NTMASGLYDH GYLLAREAIA DHDPNAGLPR QRLWRIRAGR IVTATGALER PLSFAGNDVP
GVMLASAVRD YIVDYAVAPG RRIAVVTNND DAYRTALAAL DAGLEVPVVL DARPEAEGPL
PRQARARGIR VEVNAGIAKV LGRKGVSGLA LCAQDGSGDS RESVDCDVIA MSGGWSPVVH
LWSHCGGKLT WREDQAAFVP DPAQPPTGAD GQGNVLPVGA AAGDLQVAEL TGDAPEAPIM
PVWVMPARAT RKARYKMWLD FQNDVKVSDV ELAAREGYHS VEHAKRYTTL GMATDQGKIS
NINGLAILSD TLGQPIAATG TTTFRPPYTP LTLGTIAAEA RDGVFQPLRK TPIHPWHVAR
GAFFEPVGLW QRPYCYPRGA ESHRDAVNRE IVAVRGGVGT LDASTLGKIV VKGPDAGRFL
DMMYTGMMST LPVGKCRYGL MCSENGFLVD DGVAVRLSED SWLCHTTTGG ADRIHAQMED
WLQCEWWDWQ VFTANVTEQY AQIAVVGPRA RAVLDKLGGM DVSDAALPFM TFAEGTLAGI
PARIYRISFS GELSFEVCVP ANRGLEMWER IHEAGAEFGI TPYGTEAMHV MRAEKGFIMI
GDETDGTVIP QDLGMNWAIS KKKPDYIGKR AQERSFMTSP DRWRLVGLES LDGRVLPDGA
YAVAKGVNAN SQRNTQGRVT STYWSPTLKA PIAMGLVQHG PERMGEVLEF PVPGDTYKAR
IVDPVFYDKE GAKANV
//