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Database: UniProt
Entry: C1KWD4
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Original site: C1KWD4 
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   29-OCT-2014, entry version 41.
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};
GN   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       {ECO:0000255|HAMAP-Rule:MF_01210}.
CC   -!- COFACTOR: Binds 4 magnesium or manganese ions per subunit.
CC       {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}.
CC   -!- SIMILARITY: Contains 2 ATP-grasp domains. {ECO:0000255|HAMAP-
CC       Rule:MF_01210}.
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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; GSDRIWY; -.
DR   OrthoDB; EOG6J1DC6; -.
DR   BioCyc; LMON568819:GJF9-2751-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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-UniPathway.
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_A; CPSase_L_chain_A; 1.
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; 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.
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. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      671    861       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
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   1070       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   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
//
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