PYRI_METJA
ID PYRI_METJA Reviewed; 149 AA.
AC Q58801;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Aspartate carbamoyltransferase regulatory chain;
GN Name=pyrI; OrderedLocusNames=MJ1406;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP CHARACTERIZATION.
RX PubMed=10748118; DOI=10.1074/jbc.m909220199;
RA Hack E.S., Vorobyova T., Sakash J.B., West J.M., Macol C.P., Herve G.,
RA Williams M.K., Kantrowitz E.R.;
RT "Characterization of the aspartate transcarbamoylase from Methanococcus
RT jannaschii.";
RL J. Biol. Chem. 275:15820-15827(2000).
CC -!- FUNCTION: Involved in allosteric regulation of aspartate
CC carbamoyltransferase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains
CC organized as two trimers (C3), and six regulatory PyrI chains organized
CC as three dimers (R2).
CC -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB99414.1; -; Genomic_DNA.
DR PIR; E64475; E64475.
DR PDB; 2YWW; X-ray; 2.00 A; A/B=1-149.
DR PDBsum; 2YWW; -.
DR AlphaFoldDB; Q58801; -.
DR SMR; Q58801; -.
DR STRING; 243232.MJ_1406; -.
DR EnsemblBacteria; AAB99414; AAB99414; MJ_1406.
DR KEGG; mja:MJ_1406; -.
DR eggNOG; arCOG04229; Archaea.
DR HOGENOM; CLU_128576_0_0_2; -.
DR InParanoid; Q58801; -.
DR OMA; CPNRNCI; -.
DR PhylomeDB; Q58801; -.
DR BRENDA; 2.1.3.2; 3260.
DR EvolutionaryTrace; Q58801; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0009347; C:aspartate carbamoyltransferase complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.70.140; -; 1.
DR HAMAP; MF_00002; Asp_carb_tr_reg; 1.
DR InterPro; IPR020545; Asp_carbamoyltransf_reg_N.
DR InterPro; IPR002801; Asp_carbamoylTrfase_reg.
DR InterPro; IPR020542; Asp_carbamoyltrfase_reg_C.
DR InterPro; IPR036792; Asp_carbatrfase_reg_C_sf.
DR InterPro; IPR036793; Asp_carbatrfase_reg_N_sf.
DR PANTHER; PTHR35805; PTHR35805; 1.
DR Pfam; PF01948; PyrI; 1.
DR Pfam; PF02748; PyrI_C; 1.
DR SUPFAM; SSF54893; SSF54893; 1.
DR SUPFAM; SSF57825; SSF57825; 1.
DR TIGRFAMs; TIGR00240; ATCase_reg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Pyrimidine biosynthesis; Reference proteome;
KW Zinc.
FT CHAIN 1..149
FT /note="Aspartate carbamoyltransferase regulatory chain"
FT /id="PRO_0000142331"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:2YWW"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:2YWW"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:2YWW"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:2YWW"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:2YWW"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:2YWW"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:2YWW"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2YWW"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2YWW"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2YWW"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2YWW"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:2YWW"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2YWW"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2YWW"
SQ SEQUENCE 149 AA; 16907 MW; 192B446466DF0ECE CRC64;
MIPMEELKVK KITNGTVIDH IDAGKALMVF KVLNVPKETS VMIAINVPSK KKGKKDILKI
EGIELKKEDV DKISLISPDV TINIIRNGKV VEKLKPQIPD EIEGTLKCTN PNCITNKEKV
RGKFKIESKN PLKIRCYYCE KFLNEVIFE
