ID PYRB_BACSU Reviewed; 304 AA.
AC P05654;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 27-MAR-2024, entry version 173.
DE RecName: Full=Aspartate carbamoyltransferase catalytic subunit {ECO:0000255|HAMAP-Rule:MF_00001};
DE EC=2.1.3.2 {ECO:0000255|HAMAP-Rule:MF_00001};
DE AltName: Full=Aspartate transcarbamylase {ECO:0000255|HAMAP-Rule:MF_00001};
DE Short=ATCase {ECO:0000255|HAMAP-Rule:MF_00001};
GN Name=pyrB {ECO:0000255|HAMAP-Rule:MF_00001}; OrderedLocusNames=BSU15490;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3015959; DOI=10.1016/s0021-9258(18)67362-4;
RA Lerner C.G., Switzer R.L.;
RT "Cloning and structure of the Bacillus subtilis aspartate transcarbamylase
RT gene (pyrB).";
RL J. Biol. Chem. 261:11156-11165(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1709162; DOI=10.1016/s0021-9258(18)31559-x;
RA Quinn C.L., Stephenson B.T., Switzer R.L.;
RT "Functional organization and nucleotide sequence of the Bacillus subtilis
RT pyrimidine biosynthetic operon.";
RL J. Biol. Chem. 266:9113-9127(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 287.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=1906175; DOI=10.1073/pnas.88.14.6087;
RA Stevens R.C., Reinisch K.M., Lipscomb W.N.;
RT "Molecular structure of Bacillus subtilis aspartate transcarbamoylase at
RT 3.0-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6087-6091(1991).
CC -!- FUNCTION: Catalyzes the condensation of carbamoyl phosphate and
CC aspartate to form carbamoyl aspartate and inorganic phosphate, the
CC committed step in the de novo pyrimidine nucleotide biosynthesis
CC pathway. {ECO:0000255|HAMAP-Rule:MF_00001}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00001};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000255|HAMAP-
CC Rule:MF_00001}.
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:0000255|HAMAP-Rule:MF_00001}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. ATCase family. {ECO:0000255|HAMAP-Rule:MF_00001,
CC ECO:0000305}.
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DR EMBL; M13128; AAA22685.1; -; Genomic_DNA.
DR EMBL; M59757; AAA21267.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13423.2; -; Genomic_DNA.
DR PIR; A25015; OWBSAC.
DR RefSeq; NP_389432.2; NC_000964.3.
DR RefSeq; WP_003245123.1; NZ_JNCM01000035.1.
DR PDB; 2AT2; X-ray; 3.00 A; A/B/C=1-300.
DR PDB; 3R7D; X-ray; 2.20 A; A/B/C=1-304.
DR PDB; 3R7F; X-ray; 2.10 A; A/B/C=1-304.
DR PDB; 3R7L; X-ray; 2.58 A; A/B/C/D/E/F=1-304.
DR PDBsum; 2AT2; -.
DR PDBsum; 3R7D; -.
DR PDBsum; 3R7F; -.
DR PDBsum; 3R7L; -.
DR AlphaFoldDB; P05654; -.
DR SMR; P05654; -.
DR STRING; 224308.BSU15490; -.
DR iPTMnet; P05654; -.
DR PaxDb; 224308-BSU15490; -.
DR EnsemblBacteria; CAB13423; CAB13423; BSU_15490.
DR GeneID; 937734; -.
DR KEGG; bsu:BSU15490; -.
DR PATRIC; fig|224308.179.peg.1688; -.
DR eggNOG; COG0540; Bacteria.
DR InParanoid; P05654; -.
DR OrthoDB; 9774690at2; -.
DR PhylomeDB; P05654; -.
DR BioCyc; BSUB:BSU15490-MONOMER; -.
DR BioCyc; MetaCyc:BSU15490-MONOMER; -.
DR BRENDA; 2.1.3.2; 658.
DR SABIO-RK; P05654; -.
DR UniPathway; UPA00070; UER00116.
DR EvolutionaryTrace; P05654; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:UniProtKB-UniRule.
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:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00670; asp_carb_tr; 1.
DR PANTHER; PTHR45753:SF6; ASPARTATE CARBAMOYLTRANSFERASE; 1.
DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00101; ATCASE.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Pyrimidine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..304
FT /note="Aspartate carbamoyltransferase catalytic subunit"
FT /id="PRO_0000113099"
FT BINDING 49
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 50
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 77
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 99
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 127
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 130
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 160
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 211
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 250
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT BINDING 251
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00001"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT CONFLICT 287
FT /note="R -> C (in Ref. 1; AAA22685 and 2; AAA21267)"
FT /evidence="ECO:0000305"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 12..26
FT /evidence="ECO:0007829|PDB:3R7F"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:3R7F"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:3R7F"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:3R7D"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:3R7F"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:3R7F"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:3R7D"
FT HELIX 106..112
FT /evidence="ECO:0007829|PDB:3R7F"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:3R7F"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:3R7D"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:3R7F"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3R7F"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3R7D"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:3R7F"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:3R7F"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:3R7D"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:3R7F"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:3R7F"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:3R7F"
FT HELIX 270..289
FT /evidence="ECO:0007829|PDB:3R7F"
SQ SEQUENCE 304 AA; 34224 MW; 3742CA07346E15FE CRC64;
MKHLTTMSEL STEEIKDLLQ TAQELKSGKT DNQLTGKFAA NLFFEPSTRT RFSFEVAEKK
LGMNVLNLDG TSTSVQKGET LYDTIRTLES IGVDVCVIRH SEDEYYEELV SQVNIPILNA
GDGCGQHPTQ SLLDLMTIYE EFNTFKGLTV SIHGDIKHSR VARSNAEVLT RLGARVLFSG
PSEWQDEENT FGTYVSMDEA VESSDVVMLL RIQNERHQSA VSQEGYLNKY GLTVERAERM
KRHAIIMHPA PVNRGVEIDD SLVESEKSRI FKQMKNGVFI RMAVIQRALQ TNVKRGEAAY
VISH
//
