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Database: UniProt
Entry: A0A0A3W5A3_9GAMM
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Original site: A0A0A3W5A3_9GAMM 
ID   A0A0A3W5A3_9GAMM        Unreviewed;       969 AA.
AC   A0A0A3W5A3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Sarcosine oxidase, subunit alpha {ECO:0000313|EMBL:KGT48510.1};
DE            EC=1.5.3.1 {ECO:0000313|EMBL:KGT48510.1};
GN   ORFNames=GW12_04510 {ECO:0000313|EMBL:KGT48510.1};
OS   Acinetobacter sp. HR7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT48510.1, ECO:0000313|Proteomes:UP000032870};
RN   [1] {ECO:0000313|EMBL:KGT48510.1, ECO:0000313|Proteomes:UP000032870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HR7 {ECO:0000313|EMBL:KGT48510.1,
RC   ECO:0000313|Proteomes:UP000032870};
RA   Ahn S., Kim B.-C.;
RT   "Genome sequencing of Acinetobacter sp. strain HR7.";
RL   Submitted (OCT-2014) 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:KGT48510.1}.
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DR   EMBL; JPQO01000032; KGT48510.1; -; Genomic_DNA.
DR   RefSeq; WP_034582897.1; NZ_JPQO01000032.1.
DR   AlphaFoldDB; A0A0A3W5A3; -.
DR   STRING; 1509403.GW12_04510; -.
DR   PATRIC; fig|1509403.3.peg.446; -.
DR   eggNOG; COG0404; Bacteria.
DR   eggNOG; COG0446; Bacteria.
DR   OrthoDB; 5287468at2; -.
DR   Proteomes; UP000032870; Unassembled WGS sequence.
DR   GO; GO:0008115; F:sarcosine oxidase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.10.20.440; 2Fe-2S iron-sulphur cluster binding domain, sarcosine oxidase, alpha subunit, N-terminal domain; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR042204; 2Fe-2S-bd_N.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
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; IPR041117; SoxA_A3.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
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   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   ECO:0000313|EMBL:KGT48510.1}.
FT   DOMAIN          170..423
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          499..583
FT                   /note="SoxA A3"
FT                   /evidence="ECO:0000259|Pfam:PF17806"
FT   DOMAIN          594..857
FT                   /note="Aminomethyltransferase folate-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01571"
FT   DOMAIN          881..961
FT                   /note="Glycine cleavage T-protein C-terminal barrel"
FT                   /evidence="ECO:0000259|Pfam:PF08669"
SQ   SEQUENCE   969 AA;  107600 MW;  D73AA1FBA2FDBB3F CRC64;
     MTKTGLDRLP APYGLLIDRD HQVQFEFDQQ RFSGFAGDSI ASALIASGRW IMSRSFKYHR
     PRAPLTMAGQ DANTLIQLPQ EPNVLADCTD IQTITTSSGQ NYSGSLLKDS DAFLGKFSKF
     MPVGFYYRSF YKPKGVWKLW EPMIRKKAGL GVLDLNFEPE YYDKAYLFTD VAVIGAGPAG
     LKAAITAADA GLKVLLIEQE KVLGGSLNYA RFDIAGQRAN QLRDELINVA EQHANITVLK
     EAVCNAWFTD HYLPVIQGKR MYKVRAKQCI VASGSFDQPV VFRNNDLPGV ILTSAVQRLI
     KLYAVKPGQK VVILTGNDDG YFAALDLLEA GIAVQALVDM RAGAANAALQ HAVSTKVQCY
     FRSTVYEAQH DRAMQHLTGV EIRQITAEGQ VSKDSIHLEC DVLAMSSGYM PVYQLLCQAG
     AKLSYDDRRA QFSITGLPKG LHITGSIHGV HAIENVLKDA EHTAQNVIRS VQEKSQFAEE
     LSFIESPVNF PWPMFEHPKG KEFVDFDEDL QIRDIINATK SGYRDVQLVK RFSTVGMGPS
     QGRHSALPTA RLVAKYTDRS VSETGVTTAR PPFTAEKLAH IAGRGFDPYR QTPMHQRHLE
     LGAKMMPAGN WQRPAFYGPA EQRLKNIERE ALNVRQNVGI IDVSTLGGLE IRGADSAEFL
     NRLYTFAFAK LPVGKTRYAV MAAEDGVVID DGVAGRISEQ HFYVTATTSG VDRIYQQMLK
     WNAQWRLNVD IANVTTAFAA VNVAGPNSRA LMQKVCTDVD FSNEAFPYLG LRLGTIQGIP
     VRLLRVGFVG ELGYEIHYPA RYGEFVWDLL MEAGKAWNMQ PFGVETQRLL RLEKGHIIIS
     QDTDGMTHPK ECDLSWAVAK SKPWFVGKRS IEILASQPLK RKLVSFVLDK NKTQPLEGHI
     VLEGENISGN ITSCEYSPSL DKIIGMAYVG IHQSVEGQTF PIRVEKGEIV QATVVKAPFY
     DPENKRQEV
//
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