ID K2MAW5_TRYCR Unreviewed; 1250 AA.
AC K2MAW5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=NADH-dependent fumarate reductase, putative {ECO:0000313|EMBL:EKF32293.1};
DE Flags: Fragment;
GN ORFNames=MOQ_003860 {ECO:0000313|EMBL:EKF32293.1};
OS Trypanosoma cruzi marinkellei.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=85056 {ECO:0000313|EMBL:EKF32293.1, ECO:0000313|Proteomes:UP000007350};
RN [1] {ECO:0000313|EMBL:EKF32293.1, ECO:0000313|Proteomes:UP000007350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EKF32293.1,
RC ECO:0000313|Proteomes:UP000007350};
RX PubMed=23035642; DOI=10.1186/1471-2164-13-531;
RA Franzen O., Talavera-Lopez C., Ochaya S., Butler C.E., Messenger L.A.,
RA Lewis M.D., Llewellyn M.S., Marinkelle C.J., Tyler K.M., Miles M.A.,
RA Andersson B.;
RT "Comparative genomic analysis of human infective Trypanosoma cruzi lineages
RT with the bat-restricted subspecies T. cruzi marinkellei.";
RL BMC Genomics 13:531-531(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EKF32293.1}.
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DR EMBL; AHKC01009923; EKF32293.1; -; Genomic_DNA.
DR AlphaFoldDB; K2MAW5; -.
DR EnsemblProtists; EKF32293; EKF32293; MOQ_003860.
DR OrthoDB; 169293at2759; -.
DR Proteomes; UP000007350; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd06183; cyt_b5_reduct_like; 1.
DR Gene3D; 3.10.520.10; ApbE-like domains; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 3.90.700.10; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR024932; ApbE.
DR InterPro; IPR003374; ApbE-like_sf.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR003953; FAD-binding_2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010960; Flavocytochrome_c.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat_sf.
DR NCBIfam; TIGR01813; flavo_cyto_c; 1.
DR PANTHER; PTHR43400:SF7; FAD_BINDING_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43400; FUMARATE REDUCTASE; 1.
DR Pfam; PF02424; ApbE; 1.
DR Pfam; PF00890; FAD_binding_2; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00406; CYTB5RDTASE.
DR SUPFAM; SSF143631; ApbE-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR SUPFAM; SSF56425; Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007350}.
FT DOMAIN 993..1098
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 602..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKF32293.1"
SQ SEQUENCE 1250 AA; 136719 MW; 7C5D8C051773BC03 CRC64;
FFCLLHFYFS VFSAAGRGGG KPKRRMFSRR RILLRSSFTI GVATGKMAIT KSLMFGAYPP
AAPATAAVRW ASSSSSSTLD NSPTILSQRS FFSGSPDAHS SASVVVVDAE LAAKERDRIA
REMLSQNMPS PHTEERLVVT LRGLEHTVPY TLRMVLNGAD EAKNGEIVAG NVLTEAFEVV
NQHLNHYNPE SEVSAINQLP VGVKHTMSEH MRCVMECCVR VYASSGACFD PATGPLVEFL
RSVMKDEKSD TESTLTEEEV EHFCLPQSFD VNITDGTIAR KHEGAKLDLG GVNKGYTVDR
VVEKLNAAGM RDVMFEWGGD CRATGVNYQH QAWAIAIVRP PPVEVVEQHA KEGVDEKKET
SQLLRLMYLD DEALCTSGDY ENVMYNPKYG VRSNIFDWKR RSLLEPVENE LAQVSIKCYS
AMYADALATA SLIKRDITKV RHMLEDWRHS RNRVTNYVTY TRQGERVARM FEIATENAEI
RKNRIAGSLP ARVIVVGGGL AGLSAAIEAT ACGAQVILLE KEPKVGGNSA KATSGINGWG
TRAQALDDIQ DNCKTFERDT HKSGLGGSTD PSLVRTLSVK SGDAISWLSS LGVPLTVLSQ
LGGHSRKRTH RAPDKADGTP VPIGFTIMRT LEQHIRTKLA DRVTILESTA VTSLLHEIKA
TPDGGREVRV RGVTYKKSDE KEFISMKLTA DAVILATGGF SNDHMSQSLI GEFAPELSGF
PTTNGPWATG DGVKLARRLG ATLVDMEKVQ LHPTGLIDPK DPANPTKYLG PEALRGSGGV
LLNKKGERFV NELDLRSVVS NAIIEQGDEY PYSNGSKFAF CVLNDAAVKL FGVNLLNFYA
NNLGLFKRVD DLQELAMLIG CDVLTLQNTL EAYESCSIST SACPFTGKVV YPCVLGPQGP
FHVAFVTPSI HYTMGGCLIS PSAEIQREHH SLNLLENQRP ILGLFGAGEV TGGVHGGNRL
GGNSLLECVV FGRIAGDRAA TILQKQVYAL SKDKWTSVVV RESRSGERFG TGSRVLRFNL
PGALQRSGLY LGQFIAIRGE WDGQQLIGYY SPITLPDERG VISILARGDK GTLREWICAM
RPGDSVEIKS CGGILIERNP AKKQFLFRGH VIRQFGLIAG GSGVAPMLQI IRAALERPYV
DTTESIRLFY TAEEYEELTY RELLNHYCKE NPDKFSVEFS LNNPPEGWTG GVGFVDRPSL
RKTLQPPSND LLIAICGPPA MQRAVKNDLL AMGYNPALVH TVDDDMQAAL
//