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Database: UniProt
Entry: A4ERW9_9RHOB
LinkDB: A4ERW9_9RHOB
Original site: A4ERW9_9RHOB 
ID   A4ERW9_9RHOB            Unreviewed;       990 AA.
AC   A4ERW9;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   SubName: Full=Sarcosine oxidase alpha subunit {ECO:0000313|EMBL:EBA18025.1};
GN   ORFNames=RSK20926_19842 {ECO:0000313|EMBL:EBA18025.1};
OS   Roseobacter sp. SK209-2-6.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=388739 {ECO:0000313|EMBL:EBA18025.1, ECO:0000313|Proteomes:UP000005964};
RN   [1] {ECO:0000313|EMBL:EBA18025.1, ECO:0000313|Proteomes:UP000005964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK209-2-6 {ECO:0000313|EMBL:EBA18025.1,
RC   ECO:0000313|Proteomes:UP000005964};
RA   Ward B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2006) 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:EBA18025.1}.
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DR   EMBL; AAYC01000002; EBA18025.1; -; Genomic_DNA.
DR   RefSeq; WP_008204923.1; NZ_AAYC01000002.1.
DR   AlphaFoldDB; A4ERW9; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0446; Bacteria.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000005964; 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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000005964}.
FT   DOMAIN          177..430
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          507..590
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          605..871
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          897..982
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   990 AA;  106546 MW;  A7E1915255688F08 CRC64;
     MSATRMSKGG RIDRSCPLRF TWDGRAYQGF AGDTLASALM ANGEVVLGRS FKYHRPRGIM
     SAGVEESGAI VTLGTGNRAE PNTKATMVEL YDGLVASGQN AWPNVRSDIG AALGLFGRFF
     SAGFYYKTFM GLPPFEWGRG TGLWMQYEKL IRKAAGMGAA SREADPDCYD HMHGFCDVLV
     VGSGPAGLNA ALRAAQQGKD VILVEQDHEL GGDLLNQADP TAETTRADLI AALEAAGVRI
     MTRTTAFGLY DYGTAGLLQR VSDHLAVKPE HSPRQRFWTV RSAATILATG ALERTVAFEN
     NDRPGVMTAN AARSYLNRYG VLPGQNIVLS TNNDSAYGVA VELAQAGAKV TLVELRAKVS
     PELAKQMRVA GVQIKTGLAP LKAIGDKAVS AVRLARPHGE AWRVAETLRC DLLLVSAGWS
     PVVNLLSHRG AKPLWDQSLA CFLPAPSVEN VTIAGSAAGH WSAEECVASG IAAADQALGL
     PVKEPVRAGW ETPIKPLYEV RLPGKKTKSF VDPQHDVTAS DVRLAHQEGF VSVEHLKRYT
     TLGMATDQGK MGNVIGLALM AEALGKEIPA VGTTRFRPPY TPVAIGALAG RNTGSHFKVL
     RRTPLHDWNL RHGATMTDAG LWHRPWYFGR TGESITEAYI REATTVRQTL GICDVSSLGK
     IAVQGPDASE FLNRIYSNAF AKLAVGKARY GIMLRDDGMV MDDGTTWRLS ENDFLLTTTT
     TGAGKVMVWL EELLQLRWPE LEVHVTSVSD QWAGVSVAGP KSRAAIAACL TDPEMISAES
     LPFMGVRETR LKSGIKCLIA RISFSGELAY ELYVPANQGE AMMDLLWAAS EPLGGCLYGL
     EALGTLRIEK GHVTGAELDG RVTIDDAGLG KMASTKKSFI GSVLRKRPEL ERADRPQLVG
     IFPKDRSESF NGGALLCKPD EISGFGEGWI TAVTHSPTLG HWIGLGYISG GHDAWQGRAV
     TATDPVRKGD VAVEIVTPHM FDPKGERMHG
//
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