PYRB_METJA
ID PYRB_METJA Reviewed; 306 AA.
AC Q58976;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
DE Short=ATCase;
GN Name=pyrB; OrderedLocusNames=MJ1581;
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 CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
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).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=10944354; DOI=10.1107/s0907444900008167;
RA Vitali J., Vorobyova T., Webster G., Kantrowitz E.R.;
RT "Crystallization and structure determination of the catalytic trimer of
RT Methanococcus jannaschii aspartate transcarbamoylase.";
RL Acta Crystallogr. D 56:1061-1063(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + L-aspartate = H(+) + N-carbamoyl-L-
CC aspartate + phosphate; Xref=Rhea:RHEA:20013, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:32814, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58228; EC=2.1.3.2;
CC Evidence={ECO:0000269|PubMed:10748118};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3.
CC {ECO:0000269|PubMed:10748118}.
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). {ECO:0000269|PubMed:10748118}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000305}.
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DR EMBL; L77117; AAB99601.1; -; Genomic_DNA.
DR PIR; D64497; D64497.
DR RefSeq; WP_010871106.1; NC_000909.1.
DR PDB; 2RGW; X-ray; 2.80 A; A/B/C/D/E/F=1-306.
DR PDB; 3E2P; X-ray; 3.00 A; A/B/C/D/E/F/I/J/K/L/M/N=1-306.
DR PDB; 4EKN; X-ray; 2.50 A; B=1-306.
DR PDBsum; 2RGW; -.
DR PDBsum; 3E2P; -.
DR PDBsum; 4EKN; -.
DR AlphaFoldDB; Q58976; -.
DR SMR; Q58976; -.
DR STRING; 243232.MJ_1581; -.
DR EnsemblBacteria; AAB99601; AAB99601; MJ_1581.
DR GeneID; 1452490; -.
DR KEGG; mja:MJ_1581; -.
DR eggNOG; arCOG00911; Archaea.
DR HOGENOM; CLU_043846_1_2_2; -.
DR InParanoid; Q58976; -.
DR OMA; FPTEREY; -.
DR OrthoDB; 51351at2157; -.
DR PhylomeDB; Q58976; -.
DR BRENDA; 2.1.3.2; 3260.
DR UniPathway; UPA00070; UER00116.
DR EvolutionaryTrace; Q58976; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_00001; Asp_carb_tr; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR PANTHER; PTHR11405:SF16; PTHR11405:SF16; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Pyrimidine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..306
FT /note="Aspartate carbamoyltransferase"
FT /id="PRO_0000113247"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 12..30
FT /evidence="ECO:0007829|PDB:4EKN"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 42..49
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 52..64
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4EKN"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3E2P"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2RGW"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:4EKN"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:4EKN"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:4EKN"
FT HELIX 281..302
FT /evidence="ECO:0007829|PDB:4EKN"
SQ SEQUENCE 306 AA; 35160 MW; CBDC31FC450CEF6A CRC64;
MKHLISMKDI GKEEILEILD EARKMEELLN TKRPLKLLEG KILATVFYEP STRTRLSFET
AMKRLGGEVI TMTDLKSSSV AKGESLIDTI RVISGYADII VLRHPSEGAA RLASEYSQVP
IINAGDGSNQ HPTQTLLDLY TIMREIGRID GIKIAFVGDL KYGRTVHSLV YALSLFENVE
MYFVSPKELR LPKDIIEDLK AKNIKFYEKE SLDDLDDDID VLYVTRIQKE RFPDPNEYEK
VKGSYKIKRE YVEGKKFIIM HPLPRVDEID YDVDDLPQAK YFKQSFYGIP VRMAILKKLI
EDNEGE
