ID D1A835_THECD Unreviewed; 313 AA.
AC D1A835;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 01-MAY-2013, entry version 28.
DE RecName: Full=Aspartate carbamoyltransferase;
DE EC=2.1.3.2;
DE AltName: Full=Aspartate transcarbamylase;
GN Name=pyrB; OrderedLocusNames=Tcur_3015;
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 /
OS NCIMB 10081).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Streptosporangineae; Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NCIMB 10081;
RX DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S.,
RA Glavina Del Rio T., Tice H., Cheng J., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Djao O., Land M., Hauser L.,
RA Chang Y., Jeffries C., Brettin T., Han C., Detter J., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA Klenk H., Kyrpides N.;
RT "Complete genome sequence of Thermomonospora curvata type strain
RT (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate
CC + N-carbamoyl-L-aspartate.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
CC -!- SIMILARITY: Belongs to the ATCase/OTCase family.
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DR EMBL; CP001738; ACY98557.1; -; Genomic_DNA.
DR RefSeq; YP_003300595.1; NC_013510.1.
DR ProteinModelPortal; D1A835; -.
DR EnsemblBacteria; ACY98557; ACY98557; Tcur_3015.
DR GeneID; 8604359; -.
DR KEGG; tcu:Tcur_3015; -.
DR PATRIC; 32515746; VBITheCur33965_3091.
DR HOGENOM; HOG000022685; -.
DR KO; K00609; -.
DR OMA; MTLNAMR; -.
DR UniPathway; UPA00070; UER00116.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:HAMAP.
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 HAMAP; MF_00001; Asp_carb_tr; 1; -.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR002082; Asp_carbamoyltransf.
DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00101; ATCASE.
DR SUPFAM; SSF53671; Asp/Orn_carbamoyltranf; 1.
DR TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW Complete proteome; Pyrimidine biosynthesis; Transferase.
SQ SEQUENCE 313 AA; 33926 MW; 349968244102B4E1 CRC64;
MKRHLISAAD LSRDDALLVL DTAEELAQIA DRSIKKLPTL RGRTVVNLFF EDSTRTRISF
EAAAKRLSAD VINFSAKGSS VSKGESLKDT ALTLEAMGAD AVVIRHSAAG APHRLATWVR
GSVINAGDGT HEHPTQALLD AFTMRRRLGD LDGRRVTIVG DVLHSRVARS NVLLLNTLGA
EVTLVAPPTL LPVAVDSWPC SVSYDLDAEL PKSDVVMMLR VQRERMNAAY FPTVREYSRR
YGLDAERVAK LPEHAIVMHP GPMNRGVEIA AEVADSPRST VTEQVTNGVS ARMAVLYLLL
GGSEPAIGKE VSE
//
