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Database: UniProt
Entry: B8H8U5
LinkDB: B8H8U5
Original site: B8H8U5 
ID   CARB_PSECP              Reviewed;        1109 AA.
AC   B8H8U5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   16-JAN-2019, entry version 76.
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=Achl_1999;
OS   Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 /
OS   CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS   chlorophenolicus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae;
OC   Pseudarthrobacter.
OX   NCBI_TaxID=452863;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 /
RC   NCIMB 13794 / A6;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Jansson J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Arthrobacter chlorophenolicus
RT   A6.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001341; ACL39973.1; -; Genomic_DNA.
DR   RefSeq; WP_015937191.1; NC_011886.1.
DR   ProteinModelPortal; B8H8U5; -.
DR   SMR; B8H8U5; -.
DR   STRING; 452863.Achl_1999; -.
DR   PRIDE; B8H8U5; -.
DR   EnsemblBacteria; ACL39973; ACL39973; Achl_1999.
DR   KEGG; ach:Achl_1999; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; MPWSRFR; -.
DR   OrthoDB; 48855at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002505; 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_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; Repeat.
FT   CHAIN         1   1109       Carbamoyl-phosphate synthase large chain.
FT                                /FTId=PRO_1000164702.
FT   DOMAIN      133    328       ATP-grasp 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      677    868       ATP-grasp 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01210}.
FT   DOMAIN      951   1096       MGS-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01202}.
FT   NP_BIND     159    216       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   NP_BIND     703    760       ATP. {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT   REGION      403    548       Oligomerization domain.
FT   REGION      549    950       Carbamoyl phosphate synthetic domain.
FT   REGION      951   1109       Allosteric domain.
FT   METAL       285    285       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       299    299       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       827    827       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       839    839       Magnesium or manganese 3.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       839    839       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
FT   METAL       841    841       Magnesium or manganese 4.
FT                                {ECO:0000255|HAMAP-Rule:MF_01210}.
SQ   SEQUENCE   1109 AA;  119243 MW;  3726EF12484B586A CRC64;
     MPKRTDLKSV LVIGSGPIVI GQAAEFDYSG TQALRVLKEE GLRVILVNSN PATIMTDPEF
     ADATYIEPIT PEVVEKIIAK ERPDAVLPTL GGQTALNTAI ALDKNGVLEK YNVELIGANI
     AAIELGEDRE KFKGVVERCG AESARSHIIH TMDEALEAAK DLGYPMVVRP SFTMGGLGSG
     LAYNEDDLRR IVGQGLQYSP TSEVLLEESI LGWKEYELEM MRDKNDNVVV VCSIENFDPV
     GVHTGDSITV APALTLTDRE YQKLRDVSIA VIREVGVDTG GCNIQFAIDP ATGRVVVIEM
     NPRVSRSSAL ASKATGFAIA KIATKLSLGY TLDEIPNDIT QKTPASFEPT LDYVVVKVPR
     FAFEKFPAAD NTLTTTMKSV GEAMAMGRNF TEALQKALRS LEQKGSQLDF SSVPEYEVAE
     LIEKAKRPTT DRLYQVQRAL LGGATVEQLF EATKIDPWFL DQLELLNEVS REIRQAGALT
     TDMLQRAKRH GFSDEQIGAL THNSEAVVRG VRQALGIRPV YKTVDTCAAE FAAYTPYHYS
     AYDEEDEVAL HSKPSILILG SGPNRIGQGI EFDYSCVHAS MALRKAGYET VMVNCNPETV
     STDYDVSTRL YFEPLTLEDV LEVIAAEERT GGVMGVFVQL GGQTPLKLAQ QLADAGVPIL
     GTSPEAIDLA EHRGAFSRVL DKAGLVSPKN GTAVSFEDAK KIADEIGYPV LVRPSYVLGG
     RGMEIVYDEP NLSRYIANAT EITPDHPVLI DRFLEDAVEI DVDALFDGTD MYLGGIMEHI
     EEAGIHSGDS ACVLPPITLG SNVVERVRTA TRAIAEGVGV RGLINIQFAL ASDVLYVLEA
     NPRASRTVPF VSKATGVQMA KAAALIGTGV TINQLRTAYK MLPETGDGST LPLDAPVAVK
     EAVLPFSRFR TPEGKVVDSL LGPEMRSTGE VMGIDKHFDT AFAKSQAGAN NALPTEGKVF
     VSVANRDKRS VIMGVKRLSD LGFEIVSTGG TADVLRRNGI AATPVRKVAE GSSAEGEGTI
     ADLVVAGEID MVFNTPSGGE ARSDGYELRA AATSIGIPCI TTVAEFNAAV QAIEAMRTYE
     WSVTSLQEHA AALGESQKAA AAKADLQHA
//
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