ID CARB_STAAN Reviewed; 1057 AA.
AC P63740; Q99UR5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 05-DEC-2018, entry version 104.
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}; Synonyms=pyrAB;
GN OrderedLocusNames=SA1046;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/S0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I.,
RA Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K.,
RA Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M.,
RA Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M.,
RA Ogasawara N., Hayashi H., Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus
RT aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RA Stenz L.;
RT "Shotgun proteomic analysis of total protein extract of S. aureus S30
RT versus N315.";
RL Submitted (NOV-2005) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of
RT S. aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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}.
DR EMBL; BA000018; BAB42298.1; -; Genomic_DNA.
DR PIR; F89892; F89892.
DR RefSeq; WP_001126259.1; NC_002745.2.
DR ProteinModelPortal; P63740; -.
DR SMR; P63740; -.
DR EnsemblBacteria; BAB42298; BAB42298; BAB42298.
DR KEGG; sau:SA1046; -.
DR HOGENOM; HOG000234582; -.
DR KO; K01955; -.
DR OMA; AVFPFNK; -.
DR BioCyc; SAUR158879:G1G21-1198-MONOMER; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000000751; 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.
DR PROSITE; PS51855; MGS; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding;
KW Complete proteome; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis; Repeat.
FT CHAIN 1 1057 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_0000145039.
FT DOMAIN 133 327 ATP-grasp 1. {ECO:0000255|HAMAP-
FT Rule:MF_01210}.
FT DOMAIN 671 861 ATP-grasp 2. {ECO:0000255|HAMAP-
FT Rule:MF_01210}.
FT DOMAIN 930 1057 MGS-like. {ECO:0000255|PROSITE-
FT ProRule:PRU01202}.
FT NP_BIND 159 216 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT NP_BIND 697 754 ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT REGION 1 401 Carboxyphosphate synthetic domain.
FT REGION 402 546 Oligomerization domain.
FT REGION 547 929 Carbamoyl phosphate synthetic domain.
FT REGION 930 1057 Allosteric domain.
FT METAL 284 284 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 298 298 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 298 298 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 300 300 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 820 820 Magnesium or manganese 3.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 832 832 Magnesium or manganese 3.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 832 832 Magnesium or manganese 4.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
FT METAL 834 834 Magnesium or manganese 4.
FT {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ SEQUENCE 1057 AA; 117172 MW; E3E179EF0591F0F8 CRC64;
MPKRNDIKTI LVIGSGPIII GQAAEFDYAG TQACLALKEE GYRVILVNSN PATIMTDKEI
ADKVYIEPLT HDFIARIIRK EQPDALLPTL GGQTGLNMAI QLHESGVLQD NNVQLLGTEL
TSIQQAEDRE MFRTLMNDLN VPVPESDIVN TVEQAFKFKE QVGYPLIVRP AFTMGGTGGG
ICHNDEELHE IVSNGLHYSP ATQCLLEKSI AGFKEIEYEV MRDKNDNAIV VCNMENIDPV
GIHTGDSIVV APSQTLSDVE YQMLRDVSLK VIRALGIEGG CNVQLALDPH SFDYYIIEVN
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEMLNPITG TSYAAFEPTL DYVISKIPRF
PFDKFEKGER ELGTQMKATG EVMAIGRTYE ESLLKAIRSL EYGVHHLGLP NGESFDLDYI
KERISHQDDE RLFFIGEAIR RGTTLEEIHN MTQIDYFFLH KFQNIIDIEH QLKEHQGDLE
YLKYAKDYGF SDKTIAHRFN MTEEEVYQLR MENDIKPVYK MVDTCAAEFE SSTPYYYGTY
ETENESIVTD KEKILVLGSG PIRIGQGVEF DYATVHAVWA IQKAGYEAII VNNNPETVST
DFSISDKLYF EPLTEEDVMN IINLEKPKGV VVQFGGQTAI NLADKLAKHG VKILGTSLEN
LNRAEDRKEF EALLRKINVP QPQGKSATSP EEALANAAEI GYPVVVRPSY VLGGRAMEIV
DNDKELENYM TQAVKASPEH PVLVDRYLTG KEIEVDAICD GETVIIPGIM EHIERAGVHS
GDSIAVYPPQ TLTEDELATL EDYTIKLAKG LNIIGLINIQ FVIAHDGVYV LEVNPRSSRT
VPFLSKITDI PMAQLAMRAI IGEKLTDMGY QEGVQPYAEG VFVKAPVFSF NKLKNVDITL
GPEMKSTGEV MGKDTTLEKA LFKGLTGSGV EVKDHGTVLM TVSDKDKEEV VKLAQRLNEV
GYKILATSGT ANKLAEYDIP AEVVGKIGGE NDLLTRIQNG DVQIVINTMT KGKEVERDGF
QIRRTTVENG IPCLTSLDTA NALTNVIESM TFTMRQM
//
