ID Q2CHK3_OCEGH Unreviewed; 993 AA.
AC Q2CHK3;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Putative sarcosine oxidase, alpha subunit {ECO:0000313|EMBL:EAR52291.1};
GN ORFNames=OG2516_02604 {ECO:0000313|EMBL:EAR52291.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR52291.1, ECO:0000313|Proteomes:UP000003635};
RN [1] {ECO:0000313|EMBL:EAR52291.1, ECO:0000313|Proteomes:UP000003635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000313|Proteomes:UP000003635};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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:EAR52291.1}.
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DR EMBL; AAOT01000005; EAR52291.1; -; Genomic_DNA.
DR RefSeq; WP_007254051.1; NZ_CH724107.1.
DR AlphaFoldDB; Q2CHK3; -.
DR STRING; 314256.OG2516_02604; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_011963_0_0_5; -.
DR OrthoDB; 5287468at2; -.
DR Proteomes; UP000003635; 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; 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:UP000003635}.
FT DOMAIN 170..422
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 511..593
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 609..874
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 900..985
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT REGION 476..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 107718 MW; ED29192CECE11C23 CRC64;
MSTRLKAGGR RVDPGKPVTF RFNGRKLKGF AGDTLASALL ANDQLLVGRS FKYHRPRGIV
ASGVEEPNAL VNLGEGARLE PNARATTTEL FDGLVARSQN HWPSLDFDVG AINARLSRLL
PAGFYYKMFM HPRPFWKHVY EPFIRKSAGL GEAPTDADAD TYEHYYAHVD VLIVGGGVAG
LQAALAAGRA GRSVLLMEQG AHWGGRTPVD GGEIDGGDAA GWIDAAVREL EGLDNVQLRL
RCMGAGVYDH GYVTGYERLM DHRPGAPGPR HRLWRVRAER IIVATGALER PLSFAGNDLP
GVMLASAVRD YIVEYGVSTG DRTVLVTNND DGYRTALAVL DAGLDVVAVL DARTSATGAL
PEQVRGRGVR VLTGKGVAKA TGGKRLEAVH VCAQAGEGAV IETIPCECLA MSGGWSPVVH
LWSHTGGKLS WDAERAFFRP DPDRAPTGAD GEAVVDIAGA ANGHLGLAAI LEDAHRAGGG
EGAPAPGTQP EEAPLHPVWM MPDNARIELR EKMWLDFQND VKVSDVRLAA QEGYESVEHT
KRYTTLGMAT DQGKLSNING LAVLAQALDE DIPAVGTTTF RPPYTPISMG AITGDARGEL
FQPIRRTVLH EWHERRGAYW EPVGHWRRPY CYPEGGESHG EAVAREVKNT RQAVGMLDAS
TLGKIVVKGP DAGRFLDMLY TNMMSTLPVG RCRYGLMCSE NGFLIDDGVV ARLDDDTWLC
HTTTGGSDRI HAHMEEWLQT EWWDWQVYTA NLTEQYAQIA VVGPKARAVL EKLGGMDVSA
DALKFMDWRD GELGGQPVRV FRISFSGELS YEIATPAGRG RELWDRLFEA GAEFGVMPYG
TEALHVMRAE KGFIMIGDET DGTVIPQDLG LGWAISKKKD DFLGKRAQER SHMTDPNRWQ
LVGLLTEDGS VLPDGAYIVE DGTNANGQRN VQGRVTSTYH SPTLGRGIAM ALLHRGPARM
GEVVEANKVD GGTVAAKVVS PVFYDPEGEK QNV
//
