LOCUS NP_012405 2214 aa linear PLN 15-SEP-2023
DEFINITION bifunctional carbamoylphosphate synthetase/aspartate
transcarbamylase [Saccharomyces cerevisiae S288C].
ACCESSION NP_012405
VERSION NP_012405.2
DBLINK BioProject: PRJNA128
DBSOURCE REFSEQ: accession NM_001181563.2
KEYWORDS RefSeq.
SOURCE Saccharomyces cerevisiae S288C
ORGANISM Saccharomyces cerevisiae S288C
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
Saccharomyces.
REFERENCE 1 (residues 1 to 2214)
AUTHORS Engel,S.R., Wong,E.D., Nash,R.S., Aleksander,S., Alexander,M.,
Douglass,E., Karra,K., Miyasato,S.R., Simison,M., Skrzypek,M.S.,
Weng,S. and Cherry,J.M.
TITLE New data and collaborations at the Saccharomyces Genome Database:
updated reference genome, alleles, and the Alliance of Genome
Resources
JOURNAL Genetics 220 (4) (2022)
PUBMED 34897464
REFERENCE 2 (residues 1 to 2214)
AUTHORS Goffeau,A., Barrell,B.G., Bussey,H., Davis,R.W., Dujon,B.,
Feldmann,H., Galibert,F., Hoheisel,J.D., Jacq,C., Johnston,M.,
Louis,E.J., Mewes,H.W., Murakami,Y., Philippsen,P., Tettelin,H. and
Oliver,S.G.
TITLE Life with 6000 genes
JOURNAL Science 274 (5287), 546 (1996)
PUBMED 8849441
REFERENCE 3 (residues 1 to 2214)
AUTHORS Galibert,F., Alexandraki,D., Baur,A., Boles,E., Chalwatzis,N.,
Chuat,J.C., Coster,F., Cziepluch,C., De Haan,M., Domdey,H.,
Durand,P., Entian,K.D., Gatius,M., Goffeau,A., Grivell,L.A.,
Hennemann,A., Herbert,C.J., Heumann,K., Hilger,F., Hollenberg,C.P.,
Huang,M.E., Jacq,C., Jauniaux,J.C., Katsoulou,C.,
Karpfinger-Hartl,L. et al.
TITLE Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
X
JOURNAL EMBO J. 15 (9), 2031-2049 (1996)
PUBMED 8641269
REFERENCE 4 (residues 1 to 2214)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (14-SEP-2023) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 5 (residues 1 to 2214)
CONSRTM Saccharomyces Genome Database
TITLE Direct Submission
JOURNAL Submitted (04-MAY-2012) Department of Genetics, Stanford
University, Stanford, CA 94305-5120, USA
REMARK Protein update by submitter
REFERENCE 6 (residues 1 to 2214)
CONSRTM Saccharomyces Genome Database
TITLE Direct Submission
JOURNAL Submitted (12-APR-2011) Department of Genetics, Stanford
University, Stanford, CA 94305-5120, USA
REMARK Sequence update by submitter
REFERENCE 7 (residues 1 to 2214)
CONSRTM Saccharomyces Genome Database
TITLE Direct Submission
JOURNAL Submitted (14-DEC-2009) Department of Genetics, Stanford
University, Stanford, CA 94305-5120, USA
COMMENT REVIEWED REFSEQ: This record has been curated by SGD. The reference
sequence is identical to DAA08671.
On Apr 26, 2011 this sequence version replaced NP_012405.1.
##Genome-Annotation-Data-START##
Annotation Provider :: SGD
Annotation Status :: Full Annotation
Annotation Version :: R64-4-1
URL :: http://www.yeastgenome.org/
##Genome-Annotation-Data-END##
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..2214
/organism="Saccharomyces cerevisiae S288C"
/strain="S288C"
/db_xref="taxon:559292"
/chromosome="X"
Protein 1..2214
/product="bifunctional carbamoylphosphate
synthetase/aspartate transcarbamylase"
/EC_number="2.1.3.2"
/EC_number="6.3.5.5"
/calculated_mol_wt=244911
Region 23..409
/region_name="CPSaseIIsmall"
/note="carbamoyl-phosphate synthase, small subunit;
TIGR01368"
/db_xref="CDD:273580"
Region 439..1485
/region_name="CPSaseII_lrg"
/note="carbamoyl-phosphate synthase, large subunit;
TIGR01369"
/db_xref="CDD:273581"
Region 1503..1830
/region_name="metallo-dependent_hydrolases"
/note="Superfamily of metallo-dependent hydrolases (also
called amidohydrolase superfamily) is a large group of
proteins that show conservation in their 3-dimensional
fold (TIM barrel) and in details of their active site. The
vast majority of the members have a...; cl00281"
/db_xref="CDD:444807"
Site order(1514,1516,1632,1656,1720)
/site_type="active"
/db_xref="CDD:238617"
Region 1904..2212
/region_name="PyrB"
/note="Aspartate carbamoyltransferase, catalytic chain
[Nucleotide transport and metabolism]; COG0540"
/db_xref="CDD:223614"
CDS 1..2214
/gene="URA2"
/locus_tag="YJL130C"
/coded_by="NM_001181563.2:1..6645"
/experiment="EXISTENCE:direct assay:GO:0004070 aspartate
carbamoyltransferase activity [PMID:10446140]"
/experiment="EXISTENCE:direct assay:GO:0004088
carbamoyl-phosphate synthase (glutamine-hydrolyzing)
activity [PMID:5776390]"
/experiment="EXISTENCE:direct assay:GO:0005737 cytoplasm
[PMID:11015727]"
/experiment="EXISTENCE:direct assay:GO:0005739
mitochondrion [PMID:14576278|PMID:16823961]"
/experiment="EXISTENCE:direct assay:GO:0006207 'de novo'
pyrimidine nucleobase biosynthetic process [PMID:181668]"
/experiment="EXISTENCE:direct assay:GO:0006541 glutamine
metabolic process [PMID:5651325]"
/experiment="EXISTENCE:direct assay:GO:0016020 membrane
[PMID:11921093]"
/experiment="EXISTENCE:direct assay:GO:0045984 negative
regulation of pyrimidine nucleobase metabolic process
[PMID:5651325]"
/experiment="EXISTENCE:mutant phenotype:GO:0004070
aspartate carbamoyltransferase activity [PMID:4550660]"
/experiment="EXISTENCE:mutant phenotype:GO:0006207 'de
novo' pyrimidine nucleobase biosynthetic process
[PMID:4550660]"
/note="Bifunctional carbamoylphosphate
synthetase/aspartate transcarbamylase; catalyzes the first
two enzymatic steps in the de novo biosynthesis of
pyrimidines; both activities are subject to feedback
inhibition by UTP"
/db_xref="GeneID:853311"
/db_xref="SGD:S000003666"
ORIGIN
1 matiaptapi tppmestgdr lvtlelkdgt vlqgysfgae ksvagelvfq tgmvgypesv
61 tdpsyegqil vityplvgny gvpdmhlrde lveelpryfe snrihiaglv ishytdeysh
121 ylaksslgkw lqnegipavy gvdtrsltkh lrdagsmlgr lsleksgsdr tisrssswrs
181 afdvpewvdp nvqnlvskvs inepklyvpp adnkhielqt gpdgkvlril aidvgmkynq
241 ircfikrgve lkvvpwnydf tkedydglfi sngpgdpsvl ddlsqrlsnv leakktpvfg
301 iclghqliar aagastlklk fgnrghnipc tstisgrcyi tsqnhgfavd vdtltsgwkp
361 lfvnanddsn egiyhselpy fsvqfhpest pgprdteflf dvfiqavkef kytqvlkpia
421 fpggllednv kahprieakk vlvlgsggls igqagefdys gsqaikalke egiytilinp
481 niatiqtskg ladkvyfvpv taefvrkvil herpdaiyvt fggqtalsvg iamkdefeal
541 gvkvlgtpid tiittedrel fsnaideine kcaksqaans vdealaavke igfpvivraa
601 yalgglgsgf annekelvdl cnvafssspq vlveksmkgw keveyevvrd afdncitvcn
661 menfdplgih tgdsivvaps qtlsdedynm lrttavnvir hlgvvgecni qyalnpvskd
721 yciievnarl srssalaska tgyplaytaa klglniplne vknsvtkstc acfepsldyc
781 vvkmprwdlk kftrvstels ssmksvgevm sigrtfeeai qkairsteya nlgfnetdld
841 ididyelnnp tdmrvfaian afakkgysvd kvwemtridk wflnklhdlv qfaekissfg
901 tkeelpslvl rqakqlgfdd rqiarfldsn evairrlrke ygitpfvkqi dtvaaefpay
961 tnylymtyna dshdlsfddh gvmvlgsgvy rigssvefdw cavtavrtlr anniktimvn
1021 ynpetvstdy deadrlyfet inlervldiy eienssgvvv smggqtsnni amtlhrenvk
1081 ilgtspdmid saenrykfsr mldqigvdqp awkeltsmde aesfaekvgy pvlvrpsyvl
1141 sgaamntvys kndlesylnq avevsrdypv vitkyienak eiemdavarn gelvmhvvse
1201 hvenagvhsg datlivppqd lapetvdriv vatakigkal kitgpyniqf iakdneikvi
1261 ecnvrasrsf pfiskvvgvn lielatkaim glpltpypve klpddyvavk vpqfsfprla
1321 gadpvlgvem astgevatfg hskyeaylks llatgfklpk knillsigsy kekqellssv
1381 qklynmgykl fatsgtadfl sehgiavqyl evlnkddddq kseysltqhl anneidlyin
1441 lpsanrfrrp asyvskgykt rrlavdysvp lvtnvkcakl lieaisrnit ldvserdaqt
1501 shrtitlpgl iniatyvpna shvikgpael kettrlfles gftycqlmpr sisgpvitdv
1561 aslkaansvs qdssytdfsf tiagtahnah svtqsaskvt alflplrelk nkitavaell
1621 nqwptekqvi aeaktadlas vllltslqnr sihitgvsnk edlalimtvk akdprvtcdv
1681 niyslfiaqd dypeavflpt kedqeffwnn ldsidafsvg alpvalanvt gnkvdvgmgi
1741 kdslplllaa veegkltidd ivlrlhdnpa kifniptqds vveidldysf rrnkrwspfn
1801 kdmnggierv vyngetlvls gelvspgakg kcivnpspas itasaelqst sakrrfsite
1861 eaiadnldaa edaipeqple qklmssrppr elvapgaiqn lirsnnpfrg rhilsikqfk
1921 rsdfhvlfav aqelraavar egvldlmkgh vittiffeps trtcssfiaa merlggrivn
1981 vnplvssvkk getlqdtirt lacysdaivm rhseemsvhi aakyspvpii nggngsrehp
2041 tqafldlfti reeigtvngi tvtfmgdlkh grtvhslcrl lmhyqvrinl vsppelrlpe
2101 glreelrkag llgvesielt phiisktdvl yctrvqeerf nspeeyarlk dtyivdnkil
2161 ahakenmaim hplprvneik eevdydhraa yfrqmkyglf vrmallamvm gvdm
//
