ID Q6F9E9_ACIAD Unreviewed; 973 AA.
AC Q6F9E9;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE SubName: Full=Sarcosine oxidase (Alpha subunit) oxidoreductase protein {ECO:0000313|EMBL:CAG69315.1};
DE EC=1.5.3.1 {ECO:0000313|EMBL:CAG69315.1};
GN Name=soxA {ECO:0000313|EMBL:CAG69315.1};
GN OrderedLocusNames=ACIAD2550 {ECO:0000313|EMBL:CAG69315.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG69315.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG69315.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; CR543861; CAG69315.1; -; Genomic_DNA.
DR RefSeq; WP_004928642.1; NC_005966.1.
DR AlphaFoldDB; Q6F9E9; -.
DR STRING; 202950.GCA_001485005_01467; -.
DR GeneID; 45234834; -.
DR KEGG; aci:ACIAD2550; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_011963_0_0_6; -.
DR OrthoDB; 5287468at2; -.
DR BioCyc; ASP62977:ACIAD_RS11585-MONOMER; -.
DR Proteomes; UP000000430; Chromosome.
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; 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:CAG69315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430}.
FT DOMAIN 169..424
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 503..587
FT /note="SoxA A3"
FT /evidence="ECO:0000259|Pfam:PF17806"
FT DOMAIN 598..861
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 885..965
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 973 AA; 107632 MW; D764FAA22DF91DFF CRC64;
MSNSVLQRLP HPYGSMIDRT QVIEFEFDQQ KYQGFAGDTI ASALIANQRW VMSRSFKYHR
PRAPLTMAGQ DANTLIQLPE EANVLADTTE IQPQLRAAGQ NFSGSLLKDS DAFLGKFSKF
MPVGFYYRAF YKPKGVWKLW EPLIRKKAGL GVLDLNFEPE YYDKAYLFHD VVVVGGGPAG
LQAALSAAEQ GAKVLLVEQE KLLGGSLNYA RFDVEGVVAD QLREQLVNAV TAHANIQVMT
QAVCNAWFTD HYLPVIQGKR MYKVRAKQCI VASGSFDQPV IFRNNDLPGV ILTSAVQRLI
KLYAVKPGQK VVILTGHDDG YLAALDMLEA GIDVVAVVDL REIPSNKEAY GAVKAKNVAC
YLGSTVFEAL HDKTMHRVHG VDIRKIVSEG QVAEDAKKLD CDVLCMSSGY MPVYQLLCQA
GGKLSYNDQK AEFHLSGLPQ GLHVTGSVEG IHAIEQVVEH AKYTGTLAAQ HALGQPLNVQ
SSSNTVLKNN PVNFPWPIFA HPKGKEFVDF DEDLQIRDIV NATKSGYRDV QLVKRFSTVG
MGPSQGRHSA LPTARLVAKS TQRSVSETGV TTARPPFTVE KLAHVAGRSF DPYRQTPMHA
QHVEAGATMM PAGNWQRPAF YGDAAHRLQH IENEVKHVRN QVGMIDVSTL GGLEIRGPDS
AEFINRLYTF GFTKLPVGKT RYAVMSNEHG VVIDDGVAAR LSEHHFYVTA TTSGVDRIYQ
QMLKWNAQWR LNLDITNVTT ALAAVNIAGP QSRAVMQKVC HDVDLSNAAF SYLGVREGSI
QGIPVRILRV GFVGELGYEI HFPARYGEFM WNHLMQAGQA FDIKPFGVES QRLLRLEKGH
IIISQDTDGM THPQEVDLGW AVARNKPWFV GKRSIAILEQ QPLKRKLVSF VLDKSQEKPL
EGHIVLEGED ISGNITSCEY SPTLDKIIGM AYVGIGQSEV GQQFPIRVEK GAMVHATVVK
APFYDPANRR QEI
//
