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FOLD_PSEAE
ID   FOLD_PSEAE              Reviewed;         284 AA.
AC   Q9I2U6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Bifunctional protein FolD {ECO:0000255|HAMAP-Rule:MF_01576};
DE   Includes:
DE     RecName: Full=Methylenetetrahydrofolate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01576};
DE              EC=1.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01576};
DE   Includes:
DE     RecName: Full=Methenyltetrahydrofolate cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01576};
DE              EC=3.5.4.9 {ECO:0000255|HAMAP-Rule:MF_01576};
GN   Name=folD {ECO:0000255|HAMAP-Rule:MF_01576}; OrderedLocusNames=PA1796;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBUNIT.
RX   PubMed=22558288; DOI=10.1371/journal.pone.0035973;
RA   Eadsforth T.C., Gardiner M., Maluf F.V., McElroy S., James D., Frearson J.,
RA   Gray D., Hunter W.N.;
RT   "Assessment of Pseudomonas aeruginosa N5,N10-methylenetetrahydrofolate
RT   dehydrogenase-cyclohydrolase as a potential antibacterial drug target.";
RL   PLoS ONE 7:E35973-E35973(2012).
CC   -!- FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to
CC       5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-
CC       methenyltetrahydrofolate to 10-formyltetrahydrofolate.
CC       {ECO:0000255|HAMAP-Rule:MF_01576, ECO:0000269|PubMed:22558288}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-
CC         methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812,
CC         ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01576, ECO:0000269|PubMed:22558288};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,10-methenyltetrahydrofolate + H2O = (6S)-10-
CC         formyltetrahydrofolate + H(+); Xref=Rhea:RHEA:23700,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57454,
CC         ChEBI:CHEBI:57455; EC=3.5.4.9; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01576, ECO:0000269|PubMed:22558288};
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC       {ECO:0000255|HAMAP-Rule:MF_01576}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01576,
CC       ECO:0000269|PubMed:22558288}.
CC   -!- SIMILARITY: Belongs to the tetrahydrofolate
CC       dehydrogenase/cyclohydrolase family. {ECO:0000255|HAMAP-Rule:MF_01576}.
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DR   EMBL; AE004091; AAG05185.1; -; Genomic_DNA.
DR   PIR; H83421; H83421.
DR   RefSeq; NP_250487.1; NC_002516.2.
DR   RefSeq; WP_003087898.1; NZ_QZGE01000003.1.
DR   PDB; 4A5O; X-ray; 2.20 A; A/B/C/D=1-284.
DR   PDBsum; 4A5O; -.
DR   AlphaFoldDB; Q9I2U6; -.
DR   SMR; Q9I2U6; -.
DR   STRING; 287.DR97_90; -.
DR   PaxDb; Q9I2U6; -.
DR   PRIDE; Q9I2U6; -.
DR   EnsemblBacteria; AAG05185; AAG05185; PA1796.
DR   GeneID; 880636; -.
DR   KEGG; pae:PA1796; -.
DR   PATRIC; fig|208964.12.peg.1863; -.
DR   PseudoCAP; PA1796; -.
DR   HOGENOM; CLU_034045_2_1_6; -.
DR   InParanoid; Q9I2U6; -.
DR   OMA; HIVGRPM; -.
DR   PhylomeDB; Q9I2U6; -.
DR   BioCyc; PAER208964:G1FZ6-1828-MON; -.
DR   BRENDA; 3.5.4.9; 5087.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004477; F:methenyltetrahydrofolate cyclohydrolase activity; IBA:GO_Central.
DR   GO; GO:0004488; F:methylenetetrahydrofolate dehydrogenase (NADP+) activity; IBA:GO_Central.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0035999; P:tetrahydrofolate interconversion; IBA:GO_Central.
DR   CDD; cd01080; NAD_bind_m-THF_DH_Cyclohyd; 1.
DR   HAMAP; MF_01576; THF_DHG_CYH; 1.
DR   InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF53223; SSF53223; 1.
DR   PROSITE; PS00766; THF_DHG_CYH_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Histidine biosynthesis; Hydrolase;
KW   Methionine biosynthesis; Multifunctional enzyme; NADP;
KW   One-carbon metabolism; Oxidoreductase; Purine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..284
FT                   /note="Bifunctional protein FolD"
FT                   /id="PRO_0000268443"
FT   BINDING         166..168
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT   BINDING         232
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01576"
FT   HELIX           8..28
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   STRAND          35..42
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           45..60
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   STRAND          64..70
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           76..87
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           107..112
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           116..118
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           125..132
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           141..152
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   STRAND          161..165
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           172..181
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   STRAND          185..189
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           196..201
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   STRAND          204..208
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   STRAND          226..229
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           246..252
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:4A5O"
FT   HELIX           263..281
FT                   /evidence="ECO:0007829|PDB:4A5O"
SQ   SEQUENCE   284 AA;  30549 MW;  22657CF7BEDE7967 CRC64;
     MTAQLIDGKA IAANLRQQIA QRVTERRQQG LRVPGLAVIL VGTDPASQVY VAHKRKDCEE
     VGFLSQAYDL PAETSQDDLL ALIDRLNDDP AIDGILVQLP LPAHLDASLL LERIHPDKDV
     DGFHPYNIGR LAQRMPLLRP CTPKGIMTLL ASTGADLYGM DAVVVGASNI VGRPMALELL
     LGGCTVTVTH RFTRDLADHV SRADLVVVAA GKPGLVKGEW IKEGAIVIDV GINRQADGRL
     VGDVEYEVAA QRASWITPVP GGVGPMTRAC LLENTLHAAE HLHD
 
 
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