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Database: UniProt
Entry: M3AZI1_PSEFD
LinkDB: M3AZI1_PSEFD
Original site: M3AZI1_PSEFD 
ID   M3AZI1_PSEFD            Unreviewed;      1016 AA.
AC   M3AZI1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EME82612.1};
GN   ORFNames=MYCFIDRAFT_163981 {ECO:0000313|EMBL:EME82612.1};
OS   Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS   fungus) (Mycosphaerella fijiensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=383855 {ECO:0000313|EMBL:EME82612.1, ECO:0000313|Proteomes:UP000016932};
RN   [1] {ECO:0000313|EMBL:EME82612.1, ECO:0000313|Proteomes:UP000016932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIRAD86 {ECO:0000313|EMBL:EME82612.1,
RC   ECO:0000313|Proteomes:UP000016932};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000256|ARBA:ARBA00004777}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       formate--tetrahydrofolate ligase family.
CC       {ECO:0000256|ARBA:ARBA00006985}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family. {ECO:0000256|ARBA:ARBA00005559}.
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DR   EMBL; KB446558; EME82612.1; -; Genomic_DNA.
DR   RefSeq; XP_007926092.1; XM_007927901.1.
DR   AlphaFoldDB; M3AZI1; -.
DR   STRING; 383855.M3AZI1; -.
DR   GeneID; 19332152; -.
DR   KEGG; pfj:MYCFIDRAFT_163981; -.
DR   eggNOG; KOG4230; Eukaryota.
DR   HOGENOM; CLU_003601_2_1_1; -.
DR   OrthoDB; 651667at2759; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000016932; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR   CDD; cd00477; FTHFS; 1.
DR   CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR   Gene3D; 3.10.410.10; Formyltetrahydrofolate synthetase, domain 3; 1.
DR   Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_01543; FTHFS; 1.
DR   HAMAP; MF_01576; THF_DHG_CYH; 1.
DR   InterPro; IPR046346; Aminoacid_DH-like_N_sf.
DR   InterPro; IPR000559; Formate_THF_ligase.
DR   InterPro; IPR020628; Formate_THF_ligase_CS.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000672; THF_DH/CycHdrlase.
DR   InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR   InterPro; IPR020867; THF_DH/CycHdrlase_CS.
DR   InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR   PANTHER; PTHR48099:SF5; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC; 1.
DR   PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR   Pfam; PF01268; FTHFS; 1.
DR   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00721; FTHFS_1; 1.
DR   PROSITE; PS00722; FTHFS_2; 1.
DR   PROSITE; PS00767; THF_DHG_CYH_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016932}.
FT   DOMAIN          78..194
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00763"
FT   DOMAIN          199..361
FT                   /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT                   NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02882"
SQ   SEQUENCE   1016 AA;  108988 MW;  86AE1A469830C3C3 CRC64;
     MIPRMIGASR LLPHRHRCLD CKFRLLPPPI SPSALAFPSV RPHLPSPARL ASLTRPPYKA
     AGLRSFSSTA AKMTAAKIDG TAIAKSLRQR ISKEVTEKQA KNLRYKPSLV IIQVGDRQDS
     STYVRMKLKA CEEANIACEL VKYDESISRY ELLEKIEQYN NDSSVHGMLV QLPLPKHINE
     YEITSAVADQ KDVDGFGAVN IGELAKKGGR PMFVPCTPKG VMALLKESGI EVRGKNAIVI
     GRSDIVGAPV SYLLRNADAT VTVCHSKTAN LKDVVKTGDI VVAALGSPGF VKGDWLKPGA
     VVIDVGTNPI PDETKKSGQR LVGDVDYESA VEVASQITPV PGGVGPMTVA MLLSNVVDAA
     DAYFAQQKSR HITPLPLKLK QPVPSDIEVS RSQHPKLINK VAAEVGIAPY ELEPYGAYKA
     KVSLDVLKRL EHRKNGRYIL VAGITPTPLG EGKSTTTIGL TQALAGQLGR IAFANVRQPS
     QGPTFGIKGG AAGGGYSQVI PMDEFNLHLT GDIHAITAAN NLLAAAIDTR MFHEATQKDA
     ALYSRLVPKK KGGREFAKVM FKRLKKLGID KTNPDDLTPE EITKFARLDI DPETITWRRV
     LDVNDRHLRG ITIGQAPTES KVEPRQTGFD ISVASECMAV LALSTDLADM RDRLGRMVVA
     SSKAGDPVTA DDIGVGGALA VLMKDAVKPN MMQTLEGTPV FVHAGPFANI SIGNSSIIAD
     RVALKLAGTE PDEDADRNGK VGFVVTEAGF DFTMGGERFM NIKCRASGLV PDVVVIVATV
     RALKVHGGGP EIKPGAQLDE VYRTENVDIL RAGCVNLAKH IANAKAYGVN VVVAINKFET
     DTDAEHQVIR EEAIKAGAED AIVANHWAEG GKGAVDLAQG IIKAAEKAKP EDFHLLYNTD
     GDIQTRIETI AKDMYGASKV SFSELAQKKL DTYTKQGYGN LPICIAKTQY SISHDPALKG
     APTGFEVPVR DVRMAAGAGY LYALAADIQT IPGLPTAPGY LNVDLDGETG EIDGLF
//
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