(data stored in ACNUC7421 zone)

SWISSPROT: A4SXM0_POLAQ

ID   A4SXM0_POLAQ            Unreviewed;      1087 AA.
AC   A4SXM0;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   08-MAY-2019, entry version 99.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000256|HAMAP-Rule:MF_01210};
GN   OrderedLocusNames=Pnuc_1018 {ECO:0000313|EMBL:ABP34234.1};
OS   Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS   QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153 {ECO:0000313|EMBL:ABP34234.1, ECO:0000313|Proteomes:UP000000231};
RN   [1] {ECO:0000313|EMBL:ABP34234.1, ECO:0000313|Proteomes:UP000000231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1
RC   {ECO:0000313|Proteomes:UP000000231};
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W.,
RA   Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Richardson P.,
RA   Bruce D., Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J.,
RA   Brettin T., Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N.,
RA   Goker M., Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
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:0000256|HAMAP-
CC         Rule:MF_01210, ECO:0000256|SAAS:SAAS01124510};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00981842};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00611658};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00981844}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS01000080}.
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:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00570548}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01210, ECO:0000256|SAAS:SAAS00570556}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}.
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DR   EMBL; CP000655; ABP34234.1; -; Genomic_DNA.
DR   RefSeq; WP_011902859.1; NC_009379.1.
DR   STRING; 312153.Pnuc_1018; -.
DR   EnsemblBacteria; ABP34234; ABP34234; Pnuc_1018.
DR   GeneID; 31481392; -.
DR   KEGG; pnu:Pnuc_1018; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   BioCyc; PNEC312153:G1G8K-1065-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000000231; 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; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; A4SXM0.
DR   SWISS-2DPAGE; A4SXM0.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981831};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981841};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710217};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000231};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00710245};
KW   Magnesium {ECO:0000256|SAAS:SAAS00981805};
KW   Manganese {ECO:0000256|SAAS:SAAS00459951};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00086100};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710285};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS01000143};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000231};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981845}.
FT   DOMAIN      133    335       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      683    878       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION        1    410       Carboxyphosphate synthetic domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      945   1087       Allosteric domain. {ECO:0000256|HAMAP-
FT                                Rule:MF_01210}.
SQ   SEQUENCE   1087 AA;  118816 MW;  ADA01EF5FDC37925 CRC64;
     MPKRSDIKSI LIIGAGPIVI GQACEFDYSG AQACKALRDE GYKVILVNSN PATIMTDPEM
     ADVTYIEPIT WEVVERIIAA EKPDAILPTM GGQTALNCAL DLHRHGVLEK YGCELIGASP
     EAIDKAEDRQ KFKNAMTKIG LGSAKSGIAH SMDEAHEVQQ HIQQETGSSG FPVVIRPSFT
     MGGSGGGIAY NREEFEEICK RGLDLSPTRE LLIEESLLGW KEFEMEVVRD RNDNCIIVCS
     IENLDPMGVH TGDSITVAPA QTLTDKEYQI MRNASIAVLR EIGVDTGGSN VQFSINPVDG
     RMIVIEMNPR VSRSSALASK ATGFPIAKIA AKLAVGYTLD ELKNDITGGA TPASFEPSID
     YVVTKIPRFA FEKFPQADSR LTTQMKSVGE VMAIGRTFQE SFQKALRGLE VGVDGLDEVS
     TDLDDIIQEI NEPGPDRIWY LADAFRMGMG LDEIYSETKV DPWFLEQIEE LITIETELKQ
     RKIDSLSAPE LRAVKQKGFS DRRLAKLLGV DASSVRAARH RLKVVPVYKR VDTCAAEFST
     NTAYMYSTYE AEHGECESRP TNKDKIMVLG GGPNRIGQGI EFDYCCVHAA LAMRDDGYET
     IMVNCNPETV STDYDTSDRL YFEPLTLEDV LEIVAKEKPK GVIVQYGGQT PLKLALDLER
     NGVPIIGTSP DMIDAAEDRE RFQKLLQDLG LRQPPNRTAR TEEEALKLAE EIGYPLVVRP
     SYVLGGRAME IVHDGRDLER YMREAVKVSH DSPVLLDRFL NDAIECDVDC ISDGTKVFIG
     GVMEHIEQAG VHSGDSACSL PPYSLSDATV EEIKRQTAAM AKGLHVIGLM NVQFAIQNVD
     GQDVIYVLEV NPRASRTVPF VSKATGLQLA KIAARCMVGQ TLEQQGIQAE VKPPYFSVKE
     AVFPFNKFPG IDPILGPEMR STGEVMGVGK TFGEALFKSQ LGAGIKLPKS GTVLLTVKDS
     DKPKAVEVAK LLHQLGFPMV ATKGTAAAIE AAGLPVKLVN KVKDGRPHIV DFIKNGEISL
     VFTTVDETRT AIADSRSIRT SAQANGVTYY TTISAARAVM DGLLASQNGS KESLEVYSLQ
     NLHRTLI
//

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