ID A0A2I2ZBF5_GORGO Unreviewed; 795 AA.
AC A0A2I2ZBF5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=formate--tetrahydrofolate ligase {ECO:0000256|ARBA:ARBA00012295};
DE EC=6.3.4.3 {ECO:0000256|ARBA:ARBA00012295};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000044350.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000044350.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000044350.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000044350.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; CABD030125031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2ZBF5; -.
DR Ensembl; ENSGGOT00000065656.1; ENSGGOP00000044350.1; ENSGGOG00000043341.1.
DR GeneTree; ENSGT00940000154746; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001519; Chromosome X.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IEA:InterPro.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR PANTHER; PTHR48099; C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED; 1.
DR PANTHER; PTHR48099:SF28; FORMATE--TETRAHYDROFOLATE LIGASE; 1.
DR Pfam; PF01268; FTHFS; 1.
DR Pfam; PF02882; THF_DHG_CYH_C; 1.
DR PRINTS; PR00085; THFDHDRGNASE.
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.
PE 3: Inferred from homology;
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 71..206
FT /note="Tetrahydrofolate dehydrogenase/cyclohydrolase
FT NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF02882"
SQ SEQUENCE 795 AA; 87065 MW; 1FE5BDAA480BF105 CRC64;
MAPAEILNRK ENSAQIRARL KNQVGNRDDS NLYIILYYTR VRSAATSRFR QYTEGVINAI
APEKDVDGLT SISAGKLARG DLNDCFIPCM PKGCLELMKE TGVQIARRHA VVVGCSKIVR
APMCDLLLSN NATVTTCHSK TANLDEEVSK GDILVVATGR PEIVKGEWIK PGNSHQLKVV
GDVAYDKARL MTVAMLMQST VESAKRFLEK FKPGKWMIQY NNLNLKTPVP RIGLLSEEVE
LYGETKAKVL LSALECLKHQ PDGKYQVVTG ITPTPLGEGK STTTIGLVQA LLAHLYQNFF
MCVRQPSQGP TFGIKGGAAG GGYSQVIPME EFNLHLTGDI HAITVSNNLV AAAIDAQIFH
ELTQTDKAIF THLVPSVNGV RKFSDIHIQR LNRLGIDKTD STTLIDEEIN RFARLDIDPE
TTAWQRVLNT NDRFLRKITI GQAPTKKSHT QTVHFDISVA SEIMAVLALT TSLEDRRERL
GKMVVASSKK GEPVSAEDLG MSGALIVLMK DTSKPNLMQR LEGTPVFVHA GPFANILVGP
EGFVVTEAGF GADIGIEKFF NIKSQYSGLH PHVVVLVATV SALKMHRGGP MVTAGMPLPK
AYIEENLELV EKGFSNLKKQ TENAGMFGIP IVVAVNAFKT DTETELDLIG CLSREQRAFD
AVKWGKGTLA LAQAVQRAGQ APSSFQLLYD LKLPVEDKIR IIAQKIYGAD NIELLLKVQH
KAEVYTKQGF GNLPICMAKT HLSLSHNAER KGVPTGFVLT IRDIHASIGA GFLYPLPCFY
DTDLDPETEQ VNGLV
//
