CARB_NEIGO
ID CARB_NEIGO Reviewed; 1071 AA.
AC Q59599;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 114.
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};
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CH811;
RX PubMed=7773412; DOI=10.1099/13500872-141-5-1183;
RA Lawson F.S., Billowes F.M., Dillon J.A.;
RT "Organization of carbamoyl-phosphate synthase genes in Neisseria
RT gonorrhoeae includes a large, variable intergenic sequence which is also
RT present in other Neisseria species.";
RL Microbiology 141:1183-1191(1995).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74996.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U11295; AAA74996.1; ALT_FRAME; Genomic_DNA.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
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_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; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Pyrimidine biosynthesis; Repeat.
FT CHAIN 1..1071
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145024"
FT DOMAIN 133..328
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 673..864
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 931..1071
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..403
FT /note="Carboxyphosphate synthetic domain"
FT REGION 404..548
FT /note="Oligomerization domain"
FT REGION 549..930
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 931..1071
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 699..756
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 823
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 835
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 835
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 837
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1071 AA; 117584 MW; 04B99981D3EB8212 CRC64;
MPKRTDLKSI LIIGAGPIVI GQACEFDYSG AQACKALREE GYKVILVNSN PATIMTDPEM
ADVTYIEPIM WQTVEKIIAK ERPDAILPTM GGQTXLNCAL DLAGNGVLAK YDVELIGATE
DAIDKAEDPG RFKEAMEKIG LSCPKSLFCH TMNEALAAQE QVGFPTLIRP SFTMGGSGGG
IAYNKDEFLA ICERGFDASP THELLIEQSV LGWKEYEMEV VRDKADNCII ICSIENFDPM
GVHTGDSITV APAETLTDKE YQIMRNASLA VLREIGVDTG GSNVQFAVNP EKGEMIVIEM
NPRVSRSSAL ASKATGFPIA KVAANWAVGF TLDELRNDIT GRRTPASFEP SIDYVVTKMA
RFAFEKFPAA DDRLTTQMKS VGEVMAMGRT IQESFQKALR GLETGLCGFN PARRRQTEIR
RELANPGPER MLFVGKAFRA AFTPEEIHEI SAIDPWFLAQ IEDLMKEEKS VSDGQLQDLD
YAALHRLKRK GFSDKRLAQL LNVSEKEVRE TRTPVKLDPV YKPVDTSAAE FATETAYLYS
TYEEECESRP SDRKKVMILG AGPNPIGQGI EFDYCSVHAA LPLRESGFET IMVNCNPETV
STDFDTSDRL YFEPLTLEDV LEIVRTENPW GVIVHYGGQT PLKLANALVE NGVNIIGTSA
DSIDAAEDRE RFQKVLNDLG LRQPPNRIAH NEEEALVKAE EIGYPLVVRP SYVLGGPAMQ
IVHSAEALQK YMREPVQVSE DSPVLLDFFL NNAIEVDVDC VSDGKDVVIG GIMQHVEQAG
IHSGDSGCSL PPYSLSEEIQ DEIRRQTKAM AYALGLVGLM NVQFAVQDAV VFVLEVNPRA
TRTVPFVSKA TGQRLAKVGA RCMAGISLKE QGVEKEVVPD FYAVKEAVFP FIKFPGVDTI
LNPEMRSTGE VMGVGRSFGE AYYKAQLGAG ERLNPTGKIF LSVREEDKER VIKTAKNFQA
LGYGICPTRG TAQYLTEHGL IVQAINKVPE GRPHIGDALK NGEIALVVNT VSSDPQSVSD
SHIIRQSALQ QRVPQYTTTA GGEAMSEGAK SRDYLGVYSV QELHGRLKNR N
