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Database: UniProt
Entry: S5Y1S8_PARAH
LinkDB: S5Y1S8_PARAH
Original site: S5Y1S8_PARAH 
ID   S5Y1S8_PARAH            Unreviewed;       975 AA.
AC   S5Y1S8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Sarcosine oxidase, subunit alpha {ECO:0000313|EMBL:AGT11427.1};
DE            EC=1.5.3.1 {ECO:0000313|EMBL:AGT11427.1};
GN   ORFNames=JCM7686_pAMI6p097 {ECO:0000313|EMBL:AGT11427.1};
OS   Paracoccus aminophilus JCM 7686.
OG   Plasmid pAMI6 {ECO:0000313|EMBL:AGT11427.1,
OG   ECO:0000313|Proteomes:UP000015480}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT11427.1, ECO:0000313|Proteomes:UP000015480};
RN   [1] {ECO:0000313|EMBL:AGT11427.1, ECO:0000313|Proteomes:UP000015480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT11427.1};
RC   PLASMID=Plasmid pAMI6 {ECO:0000313|Proteomes:UP000015480};
RX   PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA   Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA   Schluter A., Puhler A., Bartosik D.;
RT   "Architecture and functions of a multipartite genome of the methylotrophic
RT   bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT   chromids.";
RL   BMC Genomics 15:124-124(2014).
CC   -!- SIMILARITY: Belongs to the GcvT family.
CC       {ECO:0000256|ARBA:ARBA00008609}.
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DR   EMBL; CP006654; AGT11427.1; -; Genomic_DNA.
DR   RefSeq; WP_020953198.1; NC_022044.1.
DR   AlphaFoldDB; S5Y1S8; -.
DR   KEGG; pami:JCM7686_pAMI6p097; -.
DR   PATRIC; fig|1367847.3.peg.4402; -.
DR   HOGENOM; CLU_011963_0_0_5; -.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000015480; Plasmid pAMI6.
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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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; PF12831; FAD_oxidored; 1.
DR   Pfam; PF13510; Fer2_4; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   Pfam; PF17806; SO_alpha_A3; 1.
DR   PIRSF; PIRSF037980; SoxA; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
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:AGT11427.1}; Plasmid {ECO:0000313|EMBL:AGT11427.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015480}.
FT   DOMAIN          491..576
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          591..855
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          880..967
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   975 AA;  105016 MW;  1BDF9F2C85C71922 CRC64;
     MTRLSGGLVD RSRSLTFSFD GKSYSGFAGD TLASALLAND VRLMGRGFKY HRPRGVFSAG
     SEEPNALVEL RGGAWQEPNT RATVAELFDG LEAKSQNRVG SLSFDLLAVN DLLSPFFAAG
     FYYKTFMWPR AFWEKIYEPM IRRAAGLGSL SMQADPDSYD SGFLHCDLLV IGGGAAGLAA
     ALTAARTGAS VILADEDFRL GGRLLAESAP LDRPASEWIA ELEKEFASLP NLRVMRRTTV
     WGAFDHGIYG AVERVSDHLV TPGKRVRQTL WRITSKRAIL AAGATERHIP FANNDRPGVM
     LAGAMRSYAN RWAVSPAQKV AIFTNNDDGH RTALDLAAKG VDITAVIDSR SGAKSQGGYR
     TIAGGQVSDS KGRLGLTKVE VTANGKTEWV DCGALGVAGG WNPNLHIASH HRERPVWNDA
     LQTFLAVEGP VGLRIVGAAA GKGSTAEALA SGAEAAQAAL ADLGITAHLP ELPKGEDHAL
     NLQPLWHVPG KGRAWVDFQN DVTVKDVKLA WQENLRPVEH LKRWTTLGMA TDQGKTSNVT
     AIAVMSELTG QSINQTGTTI FRPPYTPVSM SVLGGGDTGS HFRPRRLTPT HPWAAAQGAV
     FVEVGQWMRA QYFPRPGETT WRETVDREVL ATRKGVGICD VTTLGKIDVQ GADAGEFLDR
     VYANAMKSLK VGMVRYGLML REDGFAWDDG TCARLSETDY VVTTTTANAG TIYKHMEFCR
     QCLWPELDVQ LISTTDAWAQ MSVAGPNARK LLERVVDGFD LSNEAFPYMA CGDLTVCGGL
     RARLFRISFS GELAYEIAVP ARYGNALMAR MIELGQDLGA TPYGTEALGV LRIEKGHAAG
     NELNGQTTAQ MLGMGKFVST KKDSIGAVLS RREGMVADPR VLVGFQPVDA SDPVVAGSHL
     FEEGAEQNTW TDEGWITSAC YSPHLGSAIG LGYLANGADR KGEVIVAANP LQGQSVRLRV
     VSAHFVDPEG GRVRD
//
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