ID A2R539_ASPNC Unreviewed; 852 AA.
AC A2R539;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Putative transferase CAF17, mitochondrial {ECO:0000256|ARBA:ARBA00018540};
DE AltName: Full=Putative transferase caf17, mitochondrial {ECO:0000256|ARBA:ARBA00016916};
GN ORFNames=An15g02590 {ECO:0000313|EMBL:CAL00413.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAL00413.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAL00413.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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DR EMBL; AM270338; CAL00413.1; -; Genomic_DNA.
DR RefSeq; XP_001396797.1; XM_001396760.1.
DR AlphaFoldDB; A2R539; -.
DR EnsemblFungi; CAL00413; CAL00413; An15g02590.
DR GeneID; 4987860; -.
DR KEGG; ang:An15g02590; -.
DR VEuPathDB; FungiDB:An15g02590; -.
DR HOGENOM; CLU_007884_11_2_1; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR13847:SF181; TRANSFERASE CAF17, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal 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:0000313|EMBL:CAL00413.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 6..379
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 382..437
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 440..720
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 750..828
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT REGION 828..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 829..852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 852 AA; 93431 MW; 184C74AE2546F414 CRC64;
MAATQRVVII GAGIVGANLA DELVSRGWQD ITVVEQGPLN LPGGSTSHAP GLVFQTNGSK
TMTRLAQYTV DKLRSLSDEN GMPCFNSIGG LEVATTPARV EELKRKLGYA RSWGVDARLL
TKEECLEKYP LLNKDLVLAG LHTPTDGLAL AARATQLLIA RTQQAGVRYR GSTLVTGIEQ
TGSRVTGVKT SQGIIPADIV ISCAGFWGVE IGAMAGVAIP LLPLAHQYAK TTTVPALANR
DVNHRPNGMN ASMPILRHQD QDLYYREHGD QVGIGYYGHR PMPVVAASLG QTPEHVDEKH
MPSRLEFTAQ DFAPAWKASQ ELLPVLRETH LEDGFNGIFS FTPDGGPLVG QASNLDGFYV
AEAVWVTHSA GVARSMAELL TDGASTIDLT ECELSRFEEV QLSRDYVNET SQQNFVEIYD
ILHPLQPRES PRQLRVSPFY EKQRALGAFF LELGGWERPF WYEANAQLLH ALPAQWQPPP
RDTWSSRYTS PITAVEAWKT RNAVAMYDLT SFHRVQVSGP GAATLLQRLT TSDITAPPGA
ITHTLLLNRQ GKIRSDIFVA RLEPDLFQIG ANTATDVAYL AVEARRQRQH TPAQWVQVSD
ITGSTCCIGL WGPRSRAVIR AVSNDDFSTT ALPYMSVKRA TIAGIPITAL RKSYVGELGW
EVQTSAEYGS RLWDALWQAG KPHGLIAAGR SAMNALRLEK GIRTYGVDMT TEHDPLEAGV
FHLVDLDKKE EYVGKAALQS AAQRKQPPLR RLRCLTIDDG HSMVMGKEPV YFGGKPVGYV
TTAVFSYTTK RPAAYAWLPG RVREGDAVVI EYFGRQVKAT VSADPLFDPR GSKLHREDTG
ADGFETPLKN RL
//
