ID C5AM97_BURGB Unreviewed; 1003 AA.
AC C5AM97;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Sarcosine oxidase subunit alpha {ECO:0000313|EMBL:ACR30948.1};
GN OrderedLocusNames=bglu_2g05010 {ECO:0000313|EMBL:ACR30948.1};
OS Burkholderia glumae (strain BGR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR30948.1, ECO:0000313|Proteomes:UP000002187};
RN [1] {ECO:0000313|EMBL:ACR30948.1, ECO:0000313|Proteomes:UP000002187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR30948.1,
RC ECO:0000313|Proteomes:UP000002187};
RX PubMed=19329631; DOI=10.1128/JB.00349-09;
RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT "Complete genome sequence of Burkholderia glumae BGR1.";
RL J. Bacteriol. 191:3758-3759(2009).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001504; ACR30948.1; -; Genomic_DNA.
DR RefSeq; WP_012733344.1; NC_012721.2.
DR AlphaFoldDB; C5AM97; -.
DR STRING; 626418.bglu_2g05010; -.
DR GeneID; 58138924; -.
DR KEGG; bgl:bglu_2g05010; -.
DR PATRIC; fig|626418.3.peg.726; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_011963_0_0_4; -.
DR Proteomes; UP000002187; Chromosome 2.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000002187}.
FT DOMAIN 170..430
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 518..600
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 615..878
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 905..994
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 1003 AA; 108641 MW; 2A914517CCD8F8DD CRC64;
MSQKDRLSAG GRINRAIPLS FTFNGRTYQG FQGDTLASAL LANGVHFVAR SFKYHRPRGI
VTADVAEPNA IVQLETGAYT VPNARATEIE LYQGLVASSV NAVPSLENDR MAINQKFARF
MPAGFYYKTF MWPRKFWPKY EEKIREAAGL GRAPEQLDAD RYDKQFAHCD VLVVGGGPTG
LAAAHAAAVS GARVILVDDQ RELGGSLLSC RAEIDGRPAL QWVEKIEAEL ARLPDVKLLT
RSTAFGYQDH NLVTVAQRLT EHQPVSMRKG SRELLWKIRA KHVILATGAH ERPLVFGNND
LPGVMLAGAV SAYIHRYGVL PGRNAVVFTN NDRGYQTALD LKAHGAKVTV VDSRQDSNGA
LPAAAKKHGV AVMNGSVVST ANGRQHVQSV EIASYANGAM GATTATLGCD LLAMSGGFSP
VLHLFAQSGG KAHWHDEKAC FVPGKALQRE TSVGAAAGEF SLARGLRLAV DAGAEAARAA
GFGAAQRPVA PQATDLAEAP LEPLWLVGRG EQVTRGPKRF VDFQNDVGAA DILLAAREGF
ESVEHVKRYT AMGFGTDQGK LGNINGMAIL ALALGKTIPE TGTTTYRPNY TPVTFGAFAG
RELGDFLDPI RKTCVHEWHV EHGALFEDVG NWKRPWYFPK PGEDLHAAVA RECLAVRNSV
GILDASTLGK IDIQGPDAVK LLNWVYTNPW NKLEVGKCRY GLMLDENGMV FDDGVTVRLG
EQHYMMTTTT GGAARVLTWL ERWLQTEWPD LKVRLSSVTD HWATFAVVGP NSRKVVQKVC
RDIDFANAAF PFMSYREGTV AGVKARVMRI SFSGELAYEI NVPANAGRAV WEAIMAAGAE
YDITPYGTET MHVLRAEKGY IIVGQDTDGS ITPHDLGMSG LVAKSKDFLG RRSLSRSDTM
RENRKQFVGL LTEDPALVLE EGGQIVEPDA SANADGLTPM IGHVTSSYYS PILKRSIALA
VVKGGLNKMG QPVAISLANG KRVVAKITSP VFYDTEGVRQ NVE
//
