SRR_DICDI
ID SRR_DICDI Reviewed; 324 AA.
AC Q54HH2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Probable serine racemase;
DE EC=4.3.1.17;
DE EC=4.3.1.18;
DE EC=5.1.1.18;
DE AltName: Full=D-serine ammonia-lyase;
DE AltName: Full=D-serine dehydratase;
DE AltName: Full=L-serine ammonia-lyase;
DE AltName: Full=L-serine dehydratase;
GN Name=srr; ORFNames=DDB_G0289463;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: May catalyze the synthesis of D-serine from L-serine. May
CC have serine dehydratase activity (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:35247; EC=5.1.1.18;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Allosterically activated by magnesium, and
CC possibly also other divalent metal cations. Allosterically activated by
CC ATP, ADP or GTP (Potential). {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000141; EAL62711.1; -; Genomic_DNA.
DR RefSeq; XP_636213.1; XM_631121.1.
DR PDB; 6LUT; X-ray; 1.35 A; A/B=1-324.
DR PDBsum; 6LUT; -.
DR AlphaFoldDB; Q54HH2; -.
DR SMR; Q54HH2; -.
DR STRING; 44689.DDB0230209; -.
DR PaxDb; Q54HH2; -.
DR EnsemblProtists; EAL62711; EAL62711; DDB_G0289463.
DR GeneID; 8627151; -.
DR KEGG; ddi:DDB_G0289463; -.
DR dictyBase; DDB_G0289463; srr.
DR eggNOG; KOG1251; Eukaryota.
DR HOGENOM; CLU_021152_4_2_1; -.
DR InParanoid; Q54HH2; -.
DR OMA; LIHPFDH; -.
DR PhylomeDB; Q54HH2; -.
DR BRENDA; 4.3.1.18; 1939.
DR Reactome; R-DDI-977347; Serine biosynthesis.
DR PRO; PR:Q54HH2; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0008721; F:D-serine ammonia-lyase activity; IDA:dictyBase.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IDA:dictyBase.
DR GO; GO:0000287; F:magnesium ion binding; ISS:dictyBase.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:dictyBase.
DR GO; GO:0030378; F:serine racemase activity; IDA:dictyBase.
DR GO; GO:0018114; F:threonine racemase activity; IBA:GO_Central.
DR GO; GO:0070179; P:D-serine biosynthetic process; IDA:dictyBase.
DR GO; GO:0036088; P:D-serine catabolic process; IDA:dictyBase.
DR GO; GO:0006565; P:L-serine catabolic process; IDA:dictyBase.
DR GO; GO:0006563; P:L-serine metabolic process; IDA:dictyBase.
DR GO; GO:0018249; P:protein dehydration; IDA:dictyBase.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IDA:dictyBase.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Isomerase; Lyase; Magnesium;
KW Metal-binding; Nucleotide-binding; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..324
FT /note="Probable serine racemase"
FT /id="PRO_0000328589"
FT ACT_SITE 56
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 81
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 236..237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 56
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:6LUT"
FT TURN 69..74
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 109..117
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 129..143
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 154..170
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 185..197
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 262..276
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 282..292
FT /evidence="ECO:0007829|PDB:6LUT"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:6LUT"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:6LUT"
SQ SEQUENCE 324 AA; 35092 MW; 531DD0C4D78E7DE4 CRC64;
MEPMATVTLK DIKEAHKRIE KYIHKTPVLT NSTINELAGK ELYFKCENLQ KTGSFKMRGA
CNAIFSLDEE ELSKGVVTHS SGNHGQALSY ASKVRCVKCY VVVPEDAPSV KLNAICGYGA
TVTKCKATLE ARESNTKQLI EQHSCKLIHP FDNLQVIAGQ GTASLELMEQ VENLDAIITP
VGGGGLLSGT CITAKSLNPN IKVFAAEPLG ADDTYRSLLS GEIQKHTPGK PNTIADGLLT
TVGSLTFPII KENCDGVILV TEDEIKYAMK LVWERMKIII EPSSATTLAA ILKQEFKDKK
DIKKVGIIIS GGNVDLSSIS KILN
