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Database: UniProt
Entry: A0A0J9E3V2_9RHOB
LinkDB: A0A0J9E3V2_9RHOB
Original site: A0A0J9E3V2_9RHOB 
ID   A0A0J9E3V2_9RHOB        Unreviewed;      1003 AA.
AC   A0A0J9E3V2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Sarcosine oxidase alpha subunit {ECO:0000313|EMBL:KMW57470.1};
DE            EC=1.5.3.1 {ECO:0000313|EMBL:KMW57470.1};
GN   ORFNames=AIOL_002435 {ECO:0000313|EMBL:KMW57470.1};
OS   Candidatus Rhodobacter lobularis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Rhodobacter.
OX   NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW57470.1, ECO:0000313|Proteomes:UP000037178};
RN   [1] {ECO:0000313|EMBL:KMW57470.1, ECO:0000313|Proteomes:UP000037178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGS {ECO:0000313|EMBL:KMW57470.1};
RA   Jourda C., Santini S., Claverie J.-M.;
RT   "Draft genome sequence of an Alphaproteobacteria species associated to the
RT   Mediterranean sponge Oscarella lobularis.";
RL   Submitted (JUN-2015) 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:KMW57470.1}.
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DR   EMBL; LFTY01000002; KMW57470.1; -; Genomic_DNA.
DR   RefSeq; WP_049643196.1; NZ_LFTY01000002.1.
DR   AlphaFoldDB; A0A0J9E3V2; -.
DR   STRING; 1675527.AIOL_002435; -.
DR   PATRIC; fig|1675527.3.peg.2556; -.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000037178; Unassembled WGS sequence.
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; 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; PR00411; PNDRDTASEI.
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:KMW57470.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037178}.
FT   DOMAIN          170..421
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          521..603
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          619..884
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          910..995
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   1003 AA;  109292 MW;  130766C7CC5B2C9E CRC64;
     MSTRLTQGGR LIDRAQRLDF TFNGKRLSGH PGDTLASALL ANGQMLMGRS FKYHRPRGPV
     ASGPEEPNAL MQIGKEGRFE PNQRATVQEL FDGLEAASQN HWPSLDHDVG VVNNYMSRFL
     TAGFYYKTFI HPRAAWKHVF EPIIRKAAGL GAAPQDRDED TYEHYHTHVD VLVVGGGIAG
     LAAARQAGAA GAQVLLVEQG AEWGGRAQVD GAEIDGMSAE DWIKKTLQEL EAMENVRLRI
     RCMGSGVYDH GYCLAYERLT DHLTEKDGPR HRLWKIRARQ VVTATGAIER PLSFACNDVP
     GVMLAGAVRD YVVNYGVSPG DRTVVVTNND DAYRTVIALK NAGLEVPCVI DARQTPASPL
     IDQVRDMGVR IEFGRGIGKV KGGKRVEGIT IGIQGGEGAV LEEIKCDAVA MSGGWSPVVH
     LWSHCGGKLV WDDAQAHFRP DPDRAPTGAD GAGFVRCAGM ANGSMSTAEV LADADAQGRA
     AAMAAGHKKR KKAAPKAATE TPAAIEPVWV MPQGAPSELR QKMWLDFQND VKVSDVQLAA
     REGFESVEHT KRYTTLGMAT DQGKLSNING LAVLSDSLGA AIPEVGTTTF RPPYTPISMG
     AIGGEARGDV FQPLRRSPMH DWHDANGAFW EPVGHWRRPY CYQRPGESVE EAVNREVLNT
     RKRLGLLDAS TLGKLIVKGP DAGKFLDMMY TNMMSTLKVG RCRYGLMCSE NGFLSDDGVV
     ARIDEDTYLC HTTSGGADRI HAHMEEWLQT EWWDWQVYVV NATEQYAQVA VVGPDARKVL
     ETIGGMDVSA EALPFMAWAD GEIGGFKVRV YRISFSGELS YEIAVDAHQG AAFWDMLMEA
     GAAYGAMPYG TEALHIMRAE KGFIMIGDET DGTVIPQDLG LHWAVSKKKD DFIGKRAQER
     SFMVDPERWQ LVGLETVDGG VLPDGAYAVA EGANANGQRN VQGRVTSTYH SPTLERGIAM
     GLVLHGPERM GEVLNFPGVD GTEQQARIVS PVFYDPEGEK QNV
//
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