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Database: UniProt
Entry: O50236
LinkDB: O50236
Original site: O50236 
ID   CARB_ZYMMO              Reviewed;        1112 AA.
AC   O50236; Q5NM19;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   05-DEC-2018, entry version 118.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000255|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000255|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000255|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000255|HAMAP-Rule:MF_01210};
GN   OrderedLocusNames=ZMO1617;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Lee J.S., Jin S.J., Kang H.L., Kang H.S.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J.,
RA   Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M.,
RA   Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y.,
RA   Kang H.L., Lee S.Y., Lee K.J., Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01210};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AE008692; Type=Frameshift; Positions=282; Evidence={ECO:0000305};
DR   EMBL; AF086791; AAC70356.1; -; Genomic_DNA.
DR   EMBL; AE008692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; T33717; T33717.
DR   ProteinModelPortal; O50236; -.
DR   SMR; O50236; -.
DR   PRIDE; O50236; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001173; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01424; MGS_CPS_II; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR033937; MGS_CPS_CarB.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW   Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW   Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1112       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_0000145070.
FT   DOMAIN      133    330       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      716    907       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      973   1112       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     742    799       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    404       Carboxyphosphate synthetic domain.
FT   REGION      405    587       Oligomerization domain.
FT   REGION      588    972       Carbamoyl phosphate synthetic domain.
FT   REGION      973   1112       Allosteric domain.
FT   METAL       287    287       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       303    303       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       866    866       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       878    878       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       878    878       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       880    880       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   CONFLICT    163    163       Missing (in Ref. 1; AAC70356).
FT                                {ECO:0000305}.
FT   CONFLICT    281    282       Missing (in Ref. 1; AAC70356).
FT                                {ECO:0000305}.
FT   CONFLICT    560    591       CAAEFEAKTPYMYSTYEAPFFGEPVCDSLPSN -> ARLNL
FT                                KPKRLICIPLMKRLSLVNLFAILCQAI (in Ref. 1;
FT                                AAC70356). {ECO:0000305}.
FT   CONFLICT    940    956       Missing (in Ref. 1; AAC70356).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1112 AA;  119529 MW;  B65A11546F8E085D CRC64;
     MPKRTDLQSI MIIGAGPIVI GQACEFDYSG TQACKALREE GYRVILVNSN PATIMTDPDM
     ADATYIEPIT PEVVARIIEK ERPDALLPTM GGQTALNTAL ALASDGTLEK FNCEMIGADA
     TAIDKAEDRL KFRQAMDKIG LESPRSSVAH SLEEALDGLD YVGLPAIIRP SFTMGGTGGG
     VAYNKEEFID IVSGGLSASP TQEVLIEESV IGWKEYEMEV VRDRHDNCII ICSIENIDPM
     GVHTGDSITV APALTMTDKE YQIMRNASIA VLREIGVETG NGGSNVQFAL NPENGRLVVI
     EMNPRVSRSS ALASKATGFP IAKVATKLAI GYTLDEITND ITGATPASFE PTIDYVVTKI
     PRFAFEKFKN AKPLLTTAMK SVGEVMAIGR SFPESLQKAL RGLENGLSGL DPVEALVGAN
     PSVIEAELAR PTPDRLLVAA QALREGLPAE KICEITHYDP WFIARLAEII AAENEVISNG
     LPLEAAAFRR LKAMGFSDKR LADLALQSAH LRGLGKAQAK GSGIVHDALQ AMTGGVTEAE
     VRTLRHSLNI RPVFKRIDSC AAEFEAKTPY MYSTYEAPFF GEPVCDSLPS NRKKVVILGG
     GPNRIGQGLE FDYCCCHACF ALEAAGYETI MVNCNPETVS TDYDTSDRLY FEPLTGEDVL
     EILHTEQKNG TLVGVIVQFG GQTPLKLAAE IEKAGIPILG TSPDAIDLAE DRERFSALVS
     ELGLLQPANG IARSRDEAIS VADKIGYPIL IRPSYVLGGR AMEIIDGPSQ LDDYIHTAVK
     VSGESPVLID QYLRDATEVD VDAVADGDDV VVAGILQHIE EAGIHSGDSA CSIPPYSLPA
     SIIEEIKSQT DKLARALKVQ GLMNIQFAVK GDKVYLIEVN PRASRTVPFV AKADGRPVAQ
     VAARVMAGEK LRNLPEISWP EGYTAVKEAV FPWARFPGVD PVLSPEMKST GEVMGIDIDF
     PMAFAKAQLA AGNALPRAGT FFISVKDSDK AQIVEPIKAL TDLGIKLVAT DGTARYLQSK
     GVPVERVNKV REGRPHIVDL IKDGAISLVV NTTEGWQSLQ DSASIRSSVV LAPVPYFTTA
     AAAIVAAEAI VAIKARELEV RSLQSYHSMK HA
//
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