ID A0A087ST31_AUXPR Unreviewed; 545 AA.
AC A0A087ST31;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Dihydropyrimidinase {ECO:0000313|EMBL:KFM28885.1};
GN ORFNames=APUTEX25_001848 {ECO:0000313|EMBL:RMZ57648.1}, F751_4049
GN {ECO:0000313|EMBL:KFM28885.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM28885.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM28885.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM28885.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
RN [2] {ECO:0000313|Proteomes:UP000279271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 25 {ECO:0000313|Proteomes:UP000279271};
RX DOI=10.1016/j.algal.2018.07.001;
RA Vogler B.W., Starkenburg S.R., Sudasinghe N., Schambach J.Y., Rollin J.A.,
RA Pattathil S., Barry A.N.;
RT "Characterization of plant carbon substrate utilization by Auxenochlorella
RT protothecoides.";
RL Algal Res. 34:37-48(2018).
RN [3] {ECO:0000313|EMBL:RMZ57648.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 25 {ECO:0000313|EMBL:RMZ57648.1};
RA Hovde B., Zhang X.;
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:RMZ57648.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 25 {ECO:0000313|EMBL:RMZ57648.1};
RA Vogler B.W., Starkenburg S.R., Sudasinghe N., Schambach J.Y., Rollin J.A.,
RA Pattathil S., Barry A.N.;
RT "Characterization of plant carbon substrate utilization by Auxenochlorella
RT protothecoides.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829}.
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DR EMBL; KL662184; KFM28885.1; -; Genomic_DNA.
DR EMBL; QOKY01000126; RMZ57648.1; -; Genomic_DNA.
DR RefSeq; XP_011401934.1; XM_011403632.1.
DR STRING; 3075.A0A087ST31; -.
DR GeneID; 23615440; -.
DR KEGG; apro:F751_4049; -.
DR eggNOG; KOG2584; Eukaryota.
DR OrthoDB; 1772494at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR Proteomes; UP000279271; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01314; D-HYD; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR02033; D-hydantoinase; 1.
DR PANTHER; PTHR11647:SF1; COLLAPSIN RESPONSE MEDIATOR PROTEIN; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000028924}.
FT DOMAIN 100..485
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT MOD_RES 198
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
SQ SEQUENCE 545 AA; 57873 MW; 3242CE3A24378552 CRC64;
MDSGADYGWW GFGSLARVFF VNEQACTILC PIPHALADHP AHQFPLLIIH RQCPNQGGTV
VNAEYSVVAD VLIRDEIIVA VKPNIQLTGG MQVLDATGKL VMPGGIDPHT HLDMPFMGQV
SCDDFASGQR AALAGGTTMH IDFVLPVEHD LLAGLEAWRK KARHGVMDYG FHMAVTSWSN
KVSRDMATVA AQGINSFKFF MAYKGSFMVE DDALLRGMER CAALGALAQV HAENGAAVAW
GQERVAARGV TAPHGHALSR PAALEDEATG RAIRLAGLAG ARLYVVHVMS GGAADEIAAA
RRHGQRVVGE TVISALALTE DSMWDSNFTV AAAHVMSPPI RSTAHRASVR QALAGGVLQI
VGTDHAVFNS TQKAAGKEDF RAIPNGVNGI EERLHVVWET MVNSGASTPS DFVRATSTAA
ARAFNIYPRK GSVAPGSDAD VIVLDPSVRH VISAATHHSA VDVNVYEGME VTGKVVLTLS
RGRLVWDGTN LNVTAGSGRF IPMPLFQSSR PDDLGAVVPG TAPTCPSGHR VKHADTQRVA
TLTYA
//
