GenomeNet

Database: UniProt
Entry: C1F1S6
LinkDB: C1F1S6
Original site: C1F1S6 
ID   CARB_ACIC5              Reviewed;        1093 AA.
AC   C1F1S6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 65.
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=ACP_0685;
OS   Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670 /
OS   NBRC 15755 / NCIMB 13165 / 161).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Acidobacterium.
OX   NCBI_TaxID=240015;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51196 / DSM 11244 / JCM 7670 / NBRC 15755 / NCIMB 13165 /
RC   161;
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B.,
RA   Coutinho P.M., Wu M., Xie G., Haft D.H., Sait M., Badger J.,
RA   Barabote R.D., Bradley B., Brettin T.S., Brinkac L.M., Bruce D.,
RA   Creasy T., Daugherty S.C., Davidsen T.M., DeBoy R.T., Detter J.C.,
RA   Dodson R.J., Durkin A.S., Ganapathy A., Gwinn-Giglio M., Han C.S.,
RA   Khouri H., Kiss H., Kothari S.P., Madupu R., Nelson K.E., Nelson W.C.,
RA   Paulsen I., Penn K., Ren Q., Rosovitz M.J., Selengut J.D.,
RA   Shrivastava S., Sullivan S.A., Tapia R., Thompson L.S., Watkins K.L.,
RA   Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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;
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}.
DR   EMBL; CP001472; ACO33826.1; -; Genomic_DNA.
DR   RefSeq; WP_015895860.1; NC_012483.1.
DR   ProteinModelPortal; C1F1S6; -.
DR   SMR; C1F1S6; -.
DR   STRING; 240015.ACP_0685; -.
DR   PRIDE; C1F1S6; -.
DR   EnsemblBacteria; ACO33826; ACO33826; ACP_0685.
DR   KEGG; aca:ACP_0685; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 48855at2; -.
DR   BioCyc; ACAP240015:G1GV4-660-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002207; Chromosome.
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_A; CPSase_L_chain_A; 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; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS51855; MGS; 1.
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; Reference proteome;
KW   Repeat.
FT   CHAIN         1   1093       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000164701.
FT   DOMAIN      143    338       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      689    880       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      953   1093       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     169    226       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     715    772       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    412       Carboxyphosphate synthetic domain.
FT   REGION      413    560       Oligomerization domain.
FT   REGION      561    952       Carbamoyl phosphate synthetic domain.
FT   REGION      953   1093       Allosteric domain.
FT   METAL       295    295       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       309    309       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       309    309       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       311    311       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       839    839       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       851    851       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       851    851       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       853    853       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1093 AA;  119227 MW;  194F156CCACC39F5 CRC64;
     MPRRNDIRKI LVIGSGPIVI GQSAEFDYSG TQACKALKAE GYEVVLVNSN PATIMTDPEL
     ADRTYIEPLT VKYLDEILRI EAEMLAASGS NGKFAVLPTV GGQTALNLAV ELADAGILDK
     YGVELIGAKL DAIKKAEDRL LFKDAMTRIG LDVPRSALVN NIRDGLEFAT KIGFPVIIRP
     SFTLGGSGGG IGYNREELME ILARGLDLSP VHECLIEESV LGWKEYELEV MRDLADNVII
     ICSIENMDPM GVHTGDSITV APAQTLTDRE YQAMRDAALL VMREIGVETG GSNVQFAVNP
     QTGRMTVIEM NPRVSRSSAL ASKATGFPIA KIAAKLAVGY TLDEIPNDIT RMTPACFEPT
     IDYVVTKIPK WQFEKFPGAD ENLGPQMKSV GEVMAIGRTF KESLMKALRS LETGKRVGAE
     VLEPRRLTQR LVTPQPERLN YVRFAFRQGL SVREVARMTS MDPWFLYQIK EITDTIAAIG
     DATFDNVSPE QLRKAKRMGI SDERLAEVWG LTGNEGVAKV RELRQGHGIR PIYKLVDTCA
     AEFESATPYF YSSYEEEDEA PQTDKRKVII LGSGPNRIGQ GIEFDYCCCH AAFALKEDGF
     EAIMVNCNPE TVSTDYDTSD RLYFEPLTLE DVLAIYEHET ANGADAGMIV QFGGQTPLNL
     ALRLKQAGVK IIGTSPESID LAEDRKSFGK LLEQLQIPQP QGATATSVEE ALASAERIGY
     PVLVRPSYVL GGRAMVIAYD AAAVSHYMKE AVEYSQERPI LIDHFLEDAV EVDVDALCDG
     TDVVIAGIMQ HIEEAGIHSG DSSCVLPAVD LAPQVLDTIR DYTRKLALSL KVIGLVNLQF
     AIQRDKVYVI EVNPRASRTV PYVSKATGVP LAKIASRLMT GRKLSEFLPE NIASGKDLGT
     GAHYYVKSPV FPWNKFPGVD TVLGPEMKST GEVMGVADNF GEAFAKAQLS AGLILPSSGT
     VFFSVNDHDK AALVPLAKQY IDLGFQIVAT EGTAKVLHKA GIQAESVYKV KEGRPNIVDL
     IKGQRIQLII NTPRGQDTFF DEQAIRRAAV LQRIPTITTI AAARAAAEGI AASQRKHITV
     NPLQLLHAGH AVK
//
DBGET integrated database retrieval system