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-APR-2013, entry version 85.
DE RecName: Full=Carbamoyl-phosphate synthase large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=carB;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CH811;
RX PubMed=7773412;
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
RT also present in other Neisseria species.";
RL Microbiology 141:1183-1191(1995).
CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit (By
CC similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC carbamoyl phosphate from bicarbonate: step 1/1.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
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 -!- SIMILARITY: Belongs to the CarB family.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74996.1; Type=Frameshift; Positions=Several;
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DR EMBL; U11295; AAA74996.1; ALT_FRAME; Genomic_DNA.
DR ProteinModelPortal; Q59599; -.
DR PRIDE; Q59599; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 2.
DR Gene3D; 3.30.470.20; -; 2.
DR Gene3D; 3.40.50.1380; -; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1; -.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR013816; ATP_grasp_subdomain_2.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
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; IPR016185; PreATP-grasp_dom.
DR Pfam; PF00289; CPSase_L_chain; 2.
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; CarbamoylP_synth_lsu_oligo; 1.
DR SUPFAM; SSF52335; MGS-like_dom; 1.
DR SUPFAM; SSF52440; PreATP-grasp-like; 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.
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 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_0000145024.
FT DOMAIN 133 328 ATP-grasp 1.
FT DOMAIN 673 864 ATP-grasp 2.
FT NP_BIND 159 216 ATP (By similarity).
FT NP_BIND 699 756 ATP (By similarity).
FT REGION 1 403 Carboxyphosphate synthetic domain.
FT REGION 404 548 Oligomerization domain.
FT REGION 549 930 Carbamoyl phosphate synthetic domain.
FT REGION 931 1071 Allosteric domain.
FT METAL 285 285 Magnesium or manganese 1 (By similarity).
FT METAL 299 299 Magnesium or manganese 1 (By similarity).
FT METAL 299 299 Magnesium or manganese 2 (By similarity).
FT METAL 301 301 Magnesium or manganese 2 (By similarity).
FT METAL 823 823 Magnesium or manganese 3 (By similarity).
FT METAL 835 835 Magnesium or manganese 3 (By similarity).
FT METAL 835 835 Magnesium or manganese 4 (By similarity).
FT METAL 837 837 Magnesium or manganese 4 (By similarity).
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
//
