ID N1V8M0_9MICC Unreviewed; 973 AA.
AC N1V8M0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Sarcosine oxidase subunit alpha {ECO:0000256|PIRNR:PIRNR037980};
DE EC=1.5.3.24 {ECO:0000256|PIRNR:PIRNR037980};
GN ORFNames=D477_008743 {ECO:0000313|EMBL:EMY34598.1};
OS Arthrobacter crystallopoietes BAB-32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY34598.1, ECO:0000313|Proteomes:UP000010729};
RN [1] {ECO:0000313|EMBL:EMY34598.1, ECO:0000313|Proteomes:UP000010729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-32 {ECO:0000313|EMBL:EMY34598.1,
RC ECO:0000313|Proteomes:UP000010729};
RX PubMed=23833141;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT Revealing Genes for Bioremediation.";
RL Genome Announc. 1:e00452-13(2013).
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:EMY34598.1}.
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DR EMBL; ANPE02000107; EMY34598.1; -; Genomic_DNA.
DR RefSeq; WP_005268607.1; NZ_ANPE02000107.1.
DR AlphaFoldDB; N1V8M0; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000010729; 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; 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; 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:UP000010729}.
FT DOMAIN 488..570
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 587..851
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 876..965
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 973 AA; 103844 MW; 271AFD2CDA0C8D19 CRC64;
MSTTQSHRLP ADRVAGGRID RGAELTFTVD GKTYKGYQGD TVASALLANG VLRCGNSMYL
DRPRGIMSAG VEETNALIHV AASGPANPVD ESMLTATTVA LREGLAARFL SGLGTMDPRD
DTARYDKKYV HADVVVVGSG PAGLAAAREA VRGGARVILI EQDAEFGGSL LSQPQAQIDG
KPAQEWTAEV LAELAAAPDC TLLKRTVAFG SYDSNYLLAN QNRTGHAGEA PEGVSRSRLW
HIRAGQIVLA PGALERPITF ANNDRPGVML AGAVRSYVNR YAVAPGRNVV FFTTNDSVYD
AVADLSAAGV KVAAVVDART ELSARAAAVR ESGVEVITGS AIVDTEGAER VSAVSVSSID
EAGSPVGDVR RIEADLLAVS GGWTPTIHLH SQRQGKSRWD DSLAAFVPVA PVANQHVAGA
LNGTYDTAHC VLEGTVAGRA AAKATGYQVS EEETLVAPSA EVRNAAAGEF RQVWLVPAAG
EEQDFSAHFV DLHRDQTVKD VLRATGAGMR SVEHVKRYTS ISTGDEQGKT SGVNVIGVIG
HALKSGDIGG IGTTTYRAPF TPVAFAALAG RKRGELFDPA RITSIQPWHV AQGALFEDVG
QWKRPWYFPK QGEDMDAAVL RECAAVRDSV GFMDATTLGK IEVRGKDAAE FLNRIYTNAY
KKLAVGMCRY GVMCTPDGMI FDDGTVMRLA EDHFLLTTTT SGAAKVLDWF EEWLQTEWPE
LDVVATSVTE QWSTIAVVGP KSRAVVAKVA PALDVTNEAF PFMAFRDTTL ASGVPARIAR
VSFSGELAYE INVPAWFGLH VWEAVAEAGA EFNITPYGTE TMHVLRAEKG FIIVGQDTDG
TVTPQDANME WIVSKAKDFV GKRSYSRIDN VREDRKQLVG VLPVDKSIRL PEGAQLVNQG
IRIAPSEAPV PMEGHVTSSY NSAALGRTFG LALVKNGRNR IGETLQAPLD GQLVDVVIAE
PVLFDPEGSR RDG
//
