ID A0A177E1U6_ALTAL Unreviewed; 1420 AA.
AC A0A177E1U6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=FTHFS-domain-containing protein {ECO:0000313|EMBL:OAG25401.1};
GN ORFNames=CC77DRAFT_926730 {ECO:0000313|EMBL:OAG25401.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG25401.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG25401.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG25401.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV441470; OAG25401.1; -; Genomic_DNA.
DR RefSeq; XP_018390822.1; XM_018533951.1.
DR STRING; 5599.A0A177E1U6; -.
DR GeneID; 29119545; -.
DR KEGG; aalt:CC77DRAFT_926730; -.
DR VEuPathDB; FungiDB:CC77DRAFT_926730; -.
DR OMA; QPIMFRR; -.
DR OrthoDB; 651667at2759; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000077248; 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; PS00766; THF_DHG_CYH_1; 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:UP000077248}.
FT DOMAIN 485..601
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00763"
FT DOMAIN 607..768
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
FT REGION 264..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1420 AA; 155318 MW; E06793CF2A94FFE9 CRC64;
MSSTSPDTVI IAAMLDRLEP LAPNEYIVAL SRGSDQFIAT PNGYTSTCLP NNLLRELCAG
YVKRITWASY GSKPGSWFFG WERRDSASAF MIGPEIPPAL RSYIQAVEAS ETLRSGIRVQ
LGAADSFVVW SGTAWACADV PAQLEARLRE GSSGFRKSNH ITNGSLRDSR TLDNIQWHAN
GSYYIKSGDR HLWNFQANLV CVEWNKLWKG ARQDERMVRI NKELAYVLIS PHTKKGETFA
FIKKHSAGLD TPYIVHFEGE PIHTNFDGDD GSDQPTLSSS PPGTDDVPFQ WATTKKSGRP
HRADSWELVL RKGEKVKVIR DMGRNWFVVT DKKDIKGFVH GSWLVFGDGA VHKDSKAAYG
QFVEDIRELL KPGQLQSFLA MTGYVDECTE RDCQLLKEDV SKLGICTHDL RALLQASGKY
SYEWLKEERN LWHPDRFARF VHPDHMERLT LMAEQMFVMY GILMETAHSS RQFSSTGFNM
AGQKIDGTAI AKSIRERLGQ KIKEKQEKNP RYRPSLKIVQ VGDRSDSSTY VRMKLKAAEE
ANIDCELVHL SEDLTEGELL YKIYEYNNDP AVHGILVQLP LPKHISEHTI TSAVADEKDV
DGFGIQSIGE LAKRGGKPLF TPCTPKGVMV LLQEAGIDIS GKNAVVLGRS DIVGSPVSYL
LKNADATVTV CHSRTKNLPE VVRQADIVIA AIGKAQFVKG DWLKPGAVVI DVGTNFIPDD
TKKSGQRLVG DVDYDSAVEV ASHITPVPGG VGPMTIAMLL QNLVDSADAT FDRQKKRKIS
PLPIRIEDPI PADHAISRKQ HPKQITTVAK EVGILPHELE PYGATKAKVD LSLLRRLEHR
RNGRYILIAG ITPTPLGEGK STTTIGVAQA LGAHLGRICF ANVRQPSMGP TFGIKGGAAG
GGYSQVIPMD QFNLHLTGDI HAITAANNLL AAAIETRMFH ENTQKDAALY KRLVPAKKGK
REFVPVMFRR LKKLGIDKTN PDDLTEEEIS KFARLDIDPE TITWRRVLDV NDRHLRKITV
GQAPTEKGQT RETGFDISVA SECMAILALS KDLSDLRERL GSVVVASSRA GDPVTCDDIG
AGGALTALLV DAIKPNMMQT LEGTPVFVHA GPFANISIGA SSVIADRLAL KLAGTEPDED
HDAQTGFVVT EAGFDFTMGG ERFFNIKCRS SGLVPDTVVI VATVRALKNH GGGPDISPGA
QLPEVYRTEN IDILRAGCVN LKKHIENAKQ YGVPVVVAIN RFATDTQAEI DVIREEAIAA
GAEDAIPANH FAEGGKGAVD LAEGIIKASA KPKPDYKLLY DVNSGTVQER METIAKKMYG
ASAVEFSELA QKKVDTYVKQ GFGNLPICVA KTQYSLSHDP SLKGAPTGFT VPIRDVRMAA
GAGYLYALAA DIQTIPGLPT APGYLNIDVD VETGEIDGMF
//
