ID CARB_LISIN Reviewed; 1070 AA.
AC Q92AH3;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 01-MAY-2013, entry version 88.
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; Synonyms=pyrAB; OrderedLocusNames=lin1949;
OS Listeria innocua serovar 6a (strain CLIP 11262).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=272626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP 11262;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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.
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DR EMBL; AL596170; CAC97179.1; -; Genomic_DNA.
DR PIR; AC1676; AC1676.
DR RefSeq; NP_471283.1; NC_003212.1.
DR ProteinModelPortal; Q92AH3; -.
DR STRING; 272626.lin1949; -.
DR EnsemblBacteria; CAC97179; CAC97179; CAC97179.
DR GeneID; 1130645; -.
DR KEGG; lin:lin1949; -.
DR PATRIC; 20300709; VBILisInn102668_1993.
DR GenoList; LIN1949; -.
DR eggNOG; COG0458; -.
DR HOGENOM; HOG000234582; -.
DR KO; K01955; -.
DR OMA; PMANLAT; -.
DR ProtClustDB; PRK05294; -.
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_0000145018.
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; 117861 MW; 9783DC3C9D8EF197 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 TTYAHFEPTL DYVVAKIPRF
AFDKFEQADR RLGTQMKATG EVMAIGRSWE EALLKAVRSL EIGADHLLLE EAENADAETL
ERKICFPEDD RLFFLAAALR RGQTIEQLHA KTKIDLFFLY KLSKTIELEN RLKENPQNEE
ILAEAKRAGF SDAFIATCWN IDEQAIYDLR KAQNLFPVYK MVDTCAAEFE STTPYFYSTY
EDENESIRSS KESVIVLGSG PIRIGQGVEF DYATVHSVWA IQQAGYEAII INNNPETVST
DFSISDKLYF EPLTLEDVMH VIEIEQPLGV VVQFGGQTAI NLADGLAKRG VKILGTSLED
TDRAENRDAF EKALEILQIP QPAGKTATSV EAAIKVATDI GYPVLVRPSY VLGGRAMEIV
ESEEALKHYM TNAVKVNPKH PVLVDRYVSG QEVEVDAISD GENVLIPGIM EHIERAGVHS
GDSIAVYPAQ RLSEQVKNTI VDYTTRLATG LNIIGMLNIQ YVVDGEEVFV IEVNPRSSRT
APFLSKITEI PMANVATRVI LGENLIDLGY TPGLAPEKQE IFVKVPVFSF AKLRSVDTSL
GPEMKSTGEV MGKDVTLEKA LYKGFVASGT TMHDYGTVLL TVADRDKEEA VELAKRFNRI
GFTIMATKGT ASTLEEAEIP VSQVKKIGEN QETLIDYIRN GQVTLVVNTL TTGKRPERDG
FQIRRESVEN GIPVCTSLDT AEAILRVLES RSFELESMNA SEVKQPKARV
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