ID CARB_LISMC Reviewed; 1070 AA.
AC C1KWD4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 01-MAY-2013, entry version 34.
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; OrderedLocusNames=Lm4b_01851;
OS Listeria monocytogenes serotype 4b (strain CLIP80459).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=568819;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP80459;
RX PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U.,
RA Goesmann A., Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P.,
RA Garrido P., Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT "Comparative genomics and transcriptomics of lineages I, II, and III
RT strains of Listeria monocytogenes.";
RL BMC Genomics 13:144-144(2012).
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 (By
CC similarity).
CC -!- SIMILARITY: Belongs to the CarB family.
CC -!- SIMILARITY: Contains 2 ATP-grasp domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; FM242711; CAS05609.1; -; Genomic_DNA.
DR RefSeq; YP_002758545.1; NC_012488.1.
DR ProteinModelPortal; C1KWD4; -.
DR STRING; 634178.Lm4b_01851; -.
DR EnsemblBacteria; CAS05609; CAS05609; Lm4b_01851.
DR GeneID; 7702573; -.
DR KEGG; lmc:Lm4b_01851; -.
DR PATRIC; 20306933; VBILisMon88360_1865.
DR HOGENOM; HOG000234582; -.
DR KO; K01955; -.
DR OMA; PMANLAT; -.
DR ProtClustDB; PRK05294; -.
DR BioCyc; LMON568819:GJF9-2751-MONOMER; -.
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; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
PE 3: Inferred from homology;
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 1070 Carbamoyl-phosphate synthase large chain.
FT /FTId=PRO_1000213877.
FT DOMAIN 133 327 ATP-grasp 1.
FT DOMAIN 671 861 ATP-grasp 2.
FT NP_BIND 159 216 ATP (By similarity).
FT NP_BIND 697 754 ATP (By similarity).
FT REGION 1 401 Carboxyphosphate synthetic domain.
FT REGION 402 546 Oligomerization domain.
FT REGION 547 929 Carbamoyl phosphate synthetic domain.
FT REGION 930 1070 Allosteric domain.
FT METAL 284 284 Magnesium or manganese 1 (By similarity).
FT METAL 298 298 Magnesium or manganese 1 (By similarity).
FT METAL 298 298 Magnesium or manganese 2 (By similarity).
FT METAL 300 300 Magnesium or manganese 2 (By similarity).
FT METAL 820 820 Magnesium or manganese 3 (By similarity).
FT METAL 832 832 Magnesium or manganese 3 (By similarity).
FT METAL 832 832 Magnesium or manganese 4 (By similarity).
FT METAL 834 834 Magnesium or manganese 4 (By similarity).
SQ SEQUENCE 1070 AA; 117762 MW; 6D66DC924DE940D5 CRC64;
MPKRDDIKTI LVIGSGPIVI GQAAEFDYAG TQACLSLKEE GYRVVLVNSN PATIMTDAEM
ADKVYIEPIT LDFVSRIIRK ERPDAILPTL GGQTGLNMAM ELSAAGILDE CNVEVLGTDL
TAIKKAEDRE AFRDLMNELG EPVPESDIIH NLDEAYTFVE RIGYPVIVRP AYTLGGSGGG
ICHNEQELIE TVTSGLKLSP VTQCLLEKSI AGFKEVEYEV MRDANNNAMV VCNMENIDPV
GIHTGDSIVV APSQTLSDRE YQLLRDVSLK IIRALEIEGG CNVQLALDPD SYNYYVIEVN
PRVSRSSALA SKATGYPIAK LAAKIAVGLT LDEVRNPVTG TTFAHFEPTL DYVVAKIPRF
AFDKFEQADR RLGTQMKATG EVMAIGRSWE EALLKAVRSL EIGADHLLLE EAENADEATL
ERKICFPEDD RLFFLAAALR RGQTIEQLHA KTKIDLFFLY KLSKTIELEN RIKENPQNQE
ILAEAKRAGF SDAFLATCWN VDEQAIYDLR KAQNLFPVYK MVDTCAAEFE STTPYFYSTY
EEENESTRSA KESVIVLGSG PIRIGQGVEF DYATVHSVWA IQQAGYEAII INNNPETVST
DFSISDKLYF EPLTLEDVMH VIEIEQPLGV VVQFGGQTAI NLADGLAKRG VKILGTSLED
TDRAENRDAF EKALGILQIP QPAGKTATSV EEAINVATDI GYPVLVRPSY VLGGRAMEIV
ESEEALKHYM TNAVKVNPKH PVLVDRYVSG QEVEVDAISD GENVLIPGIM EHIERAGVHS
GDSIAVYPAQ RLSSQVKNTI VDYTTRLATG LNIIGMLNIQ YVVDGEEVFV IEVNPRSSRT
APFLSKITEI PMANVATRVI LGENLIDLGY TPGLAPEKQE IFVKVPVFSF AKLRSVDTSL
GPEMKSTGEV MGKDVTLEKA LYKGFVASGT TMHDYGTVLL TVADRDKEEA VELAKRFNRI
GFTIMATKGT ASTLEEADIP VSQVKKIGEN QETLIDYIRN GQVTLVVNTL TTGKRPERDG
FQIRRESVEN GIPVCTSLDT AEAILRVLES RSFELESMNT SEVKQPKARV
//
