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Database: UniProt
Entry: A3YG70_9GAMM
LinkDB: A3YG70_9GAMM
Original site: A3YG70_9GAMM 
ID   A3YG70_9GAMM            Unreviewed;      1005 AA.
AC   A3YG70;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 73.
DE   SubName: Full=Sarcosine oxidase, alpha subunit {ECO:0000313|EMBL:EAQ63845.1};
GN   ORFNames=MED121_05643 {ECO:0000313|EMBL:EAQ63845.1};
OS   Marinomonas sp. MED121.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=314277 {ECO:0000313|EMBL:EAQ63845.1, ECO:0000313|Proteomes:UP000003436};
RN   [1] {ECO:0000313|EMBL:EAQ63845.1, ECO:0000313|Proteomes:UP000003436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED121 {ECO:0000313|EMBL:EAQ63845.1,
RC   ECO:0000313|Proteomes:UP000003436};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (JAN-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:EAQ63845.1}.
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DR   EMBL; AANE01000017; EAQ63845.1; -; Genomic_DNA.
DR   RefSeq; WP_009835362.1; NZ_CH672433.1.
DR   AlphaFoldDB; A3YG70; -.
DR   STRING; 314277.MED121_05643; -.
DR   HOGENOM; CLU_011963_0_0_6; -.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000003436; 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; 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; 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}.
FT   DOMAIN          170..424
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          521..604
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          620..884
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          911..997
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   1005 AA;  109499 MW;  8ECABD4A1B9FB90B CRC64;
     MSQNKRLDSG GRIDRKKVIN FSFDGKSYKG FDGDTLASAL LANGVDIIAR SFKYSRPRGI
     TGHGSEEPNG VIQLGTGAST IPNVRATQQE LYAGLVANPV AGWPSVNFDL MATLGKAGAM
     MPPGFYYKTF MYPQKLWMTY EHFIRKAAGL GKAPTAPDPD TYDKVNHHCD VMIVGAGPAG
     LSAALAAAKT GARVIIADEQ NEMGGSLLST TQMINGAPAS AWLKDTIEAL EDYSNVNVLP
     RSTVMGYYDH NFLAVIERRT DHLGEISPRG ARQRMHRVRA KQVILAPGAQ ERPLIFANND
     IPGVMLASSI SVYLNRYAVA PGNALVVSTA NDSGYQAAID WHKAGRKVIG IADSRAQSSG
     ELVEEAKKLG LKIWFSHAVI EAKGSRRVYA ATVAPINAEG TQVTGASQNY DCDIIATSGG
     WSPVVHLSCH TGSRPVWNDD IIGFLPGKTV QKQHCVGSLM GQHQLSDSLE QGLVIGAQAA
     CEAGFGDGSN SIKVPSVDLV KTGQAQALFL VPHSKSVSRA PKQFVDMQND VTAAGIELAT
     REGFESIEHV KRYTALGFGT DQGKLGNING MAVAAQSLNK TIAETGTTIF RPSYTPTTFG
     AIAGRDTDSL FDPIRYTAMQ SWHEANGALF EDVGQWKRPW YFPKPGETMQ QTLDRECLAT
     RNSVGILDAS TLGKIDIQGK DAREFLNRVY TNAWSKLAVG KCRYGLMLKE DGMIMDDGVT
     SCIADDHFIL TTTTGGAANV LEWLELWHQT EWPELDVYMT SVTDHWSTMT ISGPNSRKVL
     AKVCDDIDLD KDSFKFMDWR SGTVAGVKSR VFRISFTGEL SYEINVQANH GLHVWEAIME
     AGKEFDITPY GTETMHVLRA EKGFIIVGQD TDGSVTPQDM DMSWCIGKNK EFSFIGKRSF
     TRPDTARTDR KQFVGLKPKD ANVILPEGAQ AVRDPNESIP MTMVGHVTSS YYSAVLGHSF
     ALAVIKDGHN RKGESVYFPL ADGRTIEAEI TDYVFYDAKG EKQHV
//
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