CARB_PSEAE
ID CARB_PSEAE Reviewed; 1073 AA.
AC P38100; Q51430;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
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}; OrderedLocusNames=PA4756;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9139926; DOI=10.1128/jb.179.9.3043-3046.1997;
RA Lu C.-D., Kwon D.-H., Abdelal A.T.;
RT "Identification of greA encoding a transcriptional elongation factor as a
RT member of the carA-orf-carB-greA operon in Pseudomonas aeruginosa PAO1.";
RL J. Bacteriol. 179:3043-3046(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=8169201; DOI=10.1128/jb.176.9.2532-2542.1994;
RA Kwon D.-H., Lu C.-D., Walthall D.A., Brown T.M., Houghton J.E.,
RA Abdelal A.T.;
RT "Structure and regulation of the carAB operon in Pseudomonas aeruginosa and
RT Pseudomonas stutzeri: no untranslated region exists.";
RL J. Bacteriol. 176:2532-2542(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RX PubMed=2153657; DOI=10.1128/jb.172.2.630-642.1990;
RA Wong S.C., Abdelal A.T.;
RT "Unorthodox expression of an enzyme: evidence for an untranslated region
RT within carA from Pseudomonas aeruginosa.";
RL J. Bacteriol. 172:630-642(1990).
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; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC 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 the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
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DR EMBL; U81259; AAB39252.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08142.1; -; Genomic_DNA.
DR EMBL; U04992; AAA19048.1; -; Unassigned_DNA.
DR EMBL; M33818; AAA25764.1; -; Genomic_DNA.
DR PIR; D55580; D55580.
DR PIR; E83051; E83051.
DR RefSeq; NP_253444.1; NC_002516.2.
DR RefSeq; WP_003095207.1; NZ_QZGE01000018.1.
DR AlphaFoldDB; P38100; -.
DR SMR; P38100; -.
DR STRING; 287.DR97_2100; -.
DR PaxDb; P38100; -.
DR PRIDE; P38100; -.
DR EnsemblBacteria; AAG08142; AAG08142; PA4756.
DR GeneID; 881743; -.
DR KEGG; pae:PA4756; -.
DR PATRIC; fig|208964.12.peg.4982; -.
DR PseudoCAP; PA4756; -.
DR HOGENOM; CLU_000513_1_0_6; -.
DR InParanoid; P38100; -.
DR OMA; IEPAGIH; -.
DR PhylomeDB; P38100; -.
DR BioCyc; PAER208964:G1FZ6-4868-MON; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IDA:PseudoCAP.
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 GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:PseudoCAP.
DR GO; GO:0006536; P:glutamate metabolic process; IDA:PseudoCAP.
DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Pyrimidine biosynthesis; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..1073
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145028"
FT DOMAIN 133..328
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 678..869
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 936..1073
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 2..403
FT /note="Carboxyphosphate synthetic domain"
FT REGION 404..553
FT /note="Oligomerization domain"
FT REGION 554..935
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 936..1073
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 704..761
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 828
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 840
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 840
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 842
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1073 AA; 117332 MW; 4AB60064EF60F7E4 CRC64;
MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPAM
ADATYIEPIK WATVAKIIEK ERPDALLPTM GGQTALNCAL DLERHGVLEK FGVEMIGANA
DTIDKAEDRS RFDKAMKDIG LACPRSGIAH SMEEAYGVLE QVGFPCIIRP SFTMGGTGGG
IAYNREEFEE ICARGLDLSP TNELLIDESL IGWKEYEMEV VRDKKDNCII VCSIENFDPM
GVHTGDSITV APAQTLTDKE YQIMRNASLA VLREIGVETG GSNVQFGICP NTGRMVVIEM
NPRVSRSSAL ASKATGFPIA KIAAKLAVGY TLDELQNDIT GGRTPASFEP AIDYVVTKIP
RFAFEKFPKA DARLTTQMKS VGEVMAIGRT FQESVQKALR GLEVGATGFD PKLDLNDPEA
DSILKRELTV PSAERVWYVA DAFRAGKSVE EVFELTRIDE WFLVQIEDLV KDEEKVKTLG
LSSIDRELMY KLKRKGFSDA RLAKLLGVTE KNLRSHRHKL KVLPVYKRVD TCAAEFATDT
AYMYSTYEEE CEANPSSREK IMILGGGPNR IGQGIEFDYC CVHAALAMRE DGYETIMVNC
NPETVSTDYD TSDRLYFEPV TLEDVLEIVR VEQPKGVIVQ YGGQTPLKLC RALEEAGVPI
IGTSPDAIDR AEDRERFQQM VQRLNLRQPA NATARSEDEA LAASKAIGYP LVVRPSYVLG
GRAMEIVYQE EELKRYMREA VQVSNDSPVL LDHFLNCAIE VDIDAVCDGE IVVIGAIMQH
IEQAGVHSGD SACSLPPYSL PQHIQDEIRE QVKKMALELG VVGLMNVQMA VQGEDIFVIE
VNPRASRTVP FVSKCVGESL AKVAARVMAG KTLAEVGFTQ EIIPPFFSVK EAVFPFAKFP
GVDPILGPEM KSTGEVMGVG DSFAEAFAKA QLGASEILPT AGCAFISVRE DDKPFAAQVA
GDLVALGFEV VATAGTARVI EAAGLPVRRV NKVTEGRPHV VDMIKNDEVT LIINTTEGRQ
SIADSYSIRR NALQHKICCT TTIAGGQAIC EALKFGPEKT VRRLQDLHAG IKA
