ID A0A2S8WIS6_9MICC Unreviewed; 970 AA.
AC A0A2S8WIS6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Sarcosine oxidase subunit alpha {ECO:0000256|PIRNR:PIRNR037980};
DE EC=1.5.3.24 {ECO:0000256|PIRNR:PIRNR037980};
GN ORFNames=CQ018_17225 {ECO:0000313|EMBL:PQZ88185.1};
OS Arthrobacter sp. MYb227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1848601 {ECO:0000313|EMBL:PQZ88185.1, ECO:0000313|Proteomes:UP000239972};
RN [1] {ECO:0000313|EMBL:PQZ88185.1, ECO:0000313|Proteomes:UP000239972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb227 {ECO:0000313|EMBL:PQZ88185.1,
RC ECO:0000313|Proteomes:UP000239972};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + O2 + sarcosine = (6R)-5,10-
CC methylene-5,6,7,8-tetrahydrofolate + glycine + H2O2;
CC Xref=Rhea:RHEA:70455, ChEBI:CHEBI:15379, ChEBI:CHEBI:15636,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:57305, ChEBI:CHEBI:57433,
CC ChEBI:CHEBI:57453; EC=1.5.3.24;
CC Evidence={ECO:0000256|PIRNR:PIRNR037980};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|PIRNR:PIRNR037980};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|PIRNR:PIRNR037980};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037980}.
CC -!- SIMILARITY: Belongs to the GcvT family. {ECO:0000256|ARBA:ARBA00008609,
CC ECO:0000256|PIRNR:PIRNR037980}.
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:PQZ88185.1}.
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DR EMBL; PCPT01000012; PQZ88185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8WIS6; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000239972; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046653; P:tetrahydrofolate metabolic process; IEA:UniProtKB-UniRule.
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; 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; 2.
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 Cytoplasm {ECO:0000256|PIRNR:PIRNR037980};
KW NAD {ECO:0000256|PIRNR:PIRNR037980};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037980};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR037980};
KW Reference proteome {ECO:0000313|Proteomes:UP000239972}.
FT DOMAIN 132..388
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 483..567
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 583..849
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 873..962
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 970 AA; 103745 MW; F9A1060704FA9B12 CRC64;
MSTPSPQRLS AEASASARID RSKPISFSVD GKQYSGFIGD SVASAMLGAG LKACGPSLYL
QRPRGIMSAG VEESNALIKV GARYAGHVNE SMLPAPAVEL TEGMDVTLLS GLGQLDPRTD
EAIYDRKHVH TDVLIVGAGP AGLAAAREAA KSGARVILID EQPEAGGSLL SASTESIDGK
SAAEWIAETR AALESAAEFT YLSRTTAFGS YDANYVVAVQ RRTDHLAGEL GAGVSRERIW
HIRANQVVLA TGAHERPLVF ENNDRPGIML AAAARSYLNR YGVLVGNNIV VATTNDSAYA
LVEDLEAAGH LVAAVIDARE EPSVRATELS ARGIRVILGS VVANTAAGSD GALASVILSG
IDAQGQLSGE TETLDADVLA VSGGWNPVVH LHSQRERRLG WNESLSAFVP AHPVPNQQTT
GAMNGRLELA SALAEGARAG ADAATAAGFS TTAAVPSAPV EQPSPTRALW LVPSLDGEGA
DYKNHFVDFQ RDQTVADVLR SVGAGMRSVE HVKRYTSIST ANDQGKTSGV NAIGVIAAAL
DINDVAGIGT TAFRAPYTPV AFAALAGRQR GELFDPARLT SIHPWHVERG ALFEDVGQWK
RPWYYPQAGE DMDTAVYRES KAVRDSVGFM DASTLGKIEI RGKDAGEFLN RMYTNAFKKL
KPGLARYGLM CKADGMIFDD GVTLRLDEDR FFMTTTTGGA AGVLDWLEEW LQTEWPELDV
KCTSVTEQYS TVAVVGPKSR AVLAKVAPEL DLDNETFPFM AFKETTLASG IEARVCRISF
SGELAYEINV PAWYGLKVWE DVAEAGEEFN ITPYGTETMH VLRAEKGFII VGQDTDGTVT
PQDASMEWVV SKVKDFIGKR SFDRVDNKRE DRKQLVTVLP TDKTLRLPEG TQLVNKGTEL
TQSVSPVPMQ GFVTSSYDSP ALGRTFGMAM IANGRARVGE ELSAFVDGRL VDVVVGETVL
FDSEGSRRDG
//
