ID S6GJZ7_9GAMM Unreviewed; 1011 AA.
AC S6GJZ7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Sarcosine oxidase, subunit alpha {ECO:0000313|EMBL:EPJ45804.1};
GN ORFNames=OFPII_24520 {ECO:0000313|EMBL:EPJ45804.1};
OS Osedax symbiont Rs1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ45804.1, ECO:0000313|Proteomes:UP000014822};
RN [1] {ECO:0000313|EMBL:EPJ45804.1, ECO:0000313|Proteomes:UP000014822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) 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:EPJ45804.1}.
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DR EMBL; ASZJ01000114; EPJ45804.1; -; Genomic_DNA.
DR AlphaFoldDB; S6GJZ7; -.
DR PATRIC; fig|1330036.3.peg.2347; -.
DR Proteomes; UP000014822; 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; 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000014822}.
FT DOMAIN 172..429
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 527..610
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 625..891
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 917..1003
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 1011 AA; 109548 MW; 9DF21B9FDC5FE121 CRC64;
MSQQNRLKSG GRIARNCQIN FSYNNQSYPG FVGDTLASAM LANGIDIVGR SFKYSRPRGI
VGAGAEEPNA IMQLGATEAT QVPNVRATQQ ELFNGLVATS TNGWPNVDFD MMGALGSIGA
KMMPPGFYYK TFMYPKSMWS SYEKYIRKAA GLGRSPRESD PDRYDHYNQH ADIVIVGAGP
AGLSAALVAA RSGARVIIAD EQAEFGGSLL DSTALIDGEP AMQWVTKVVA ELAACPEVLM
LPRATVNGYH DHNFLTIHER CTDHIADRAP TNTSKQRMHR VRSRWVVLAT GSHERPLVFA
NNDVPGCMLA AAVSTYINRY AVVPGNQLVL MTTNDNAYAA AFDWHAAGRE VVAIVDTRSG
GAGVQVADKA KSLGIRVISG AAVVEVQGSK RVASVSVSAL NSVGDKLTGT LEQLKCDTLA
SSGGWSPAIH LSCHTGSRPV WSDQVIGFIP GKTVQKQLVV GAINGTFDLH SCLADGTATG
EQAVLNAGFK LASGSADSGA ASTEIVTENP PMALYHIPHP KPTSRAPKQF VDLQNDVTAA
GIEMATLEGF ESIEHVKRYT AMGFGTDQGK MGNINGMAIA AKSMRKTIPE TGTTIFRPNY
TPVTFGAIAG RHCAGLFDPM RFSAMHEWHM ENGALFEDVG NWKRPWYFPQ AGESMQQALE
RECLAVRESA GVLDASTLGK IDIQGPDARE FLGRVYANAW AKLAIGKCRY GLMCGEDGMV
FDDGVTACLA ENHFIMTTTT GGAARVLEWL EIYQQTEWPE LDVYFNTVTD HFSTVTVTGP
KARKILEAVV DDIDLSNDAF KYMDWKVATV QGIPARIFRI SFTGELSFEI NVQANYGLRI
WQAVMEKGAA YNLTPYGTET MHILRAEKGF IIAGQDTDGS VHPYDLGMGW AVSTKKAFSF
IGKRGMQRAD CVKEDRKQMV GLKTKDPLQV IPEGSQAVND PNQPIPMTML GHVTSSYYSA
CLGHSIAMAF IRNGHNRMGE TVFYPQPDGT AIEAIICSPI FLDPKGERQN V
//
