ID   F9RWV3_9VIBR            Unreviewed;      1076 AA.
AC   F9RWV3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   25-JAN-2012, entry version 3.
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; ORFNames=VII00023_13697;
OS   Vibrio ichthyoenteri ATCC 700023.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=870968;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 700023;
RA   Strain E.A., Brown E., Allard M.W.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data.
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DR   EMBL; AFWF01000007; EGU48867.1; -; Genomic_DNA.
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:0006526; P:arginine biosynthetic process; IEA:HAMAP.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
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; IPR005479; CarbamoylP_synth_lsu_ATP-bd.
DR   InterPro; IPR005483; CarbamoylP_synth_lsu_CPS-dom.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 2.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
DR   Gene3D; G3DSA:1.10.1030.10; CarbamoylP_synth_lsu_oligo; 1.
DR   Gene3D; G3DSA:3.40.50.1380; MGS-like_dom; 1.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 2.
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; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Repeat.
FT   DOMAIN      133    328       ATP-grasp 1 (By similarity).
FT   DOMAIN      678    869       ATP-grasp 2 (By similarity).
FT   NP_BIND     159    216       ATP (By similarity).
FT   NP_BIND     704    761       ATP (By similarity).
FT   REGION        1    403       Carboxyphosphate synthetic domain (By
FT                                similarity).
FT   REGION      404    553       Oligomerization domain (By similarity).
FT   REGION      554    935       Carbamoyl phosphate synthetic domain (By
FT                                similarity).
FT   REGION      936   1076       Allosteric domain (By similarity).
FT   METAL       285    285       Magnesium or manganese 1 (By similarity).
FT   METAL       299    299       Magnesium or manganese 1 (By similarity).
FT   METAL       299    299       Magnesium or manganese 2 (By similarity).
FT   METAL       301    301       Magnesium or manganese 2 (By similarity).
FT   METAL       828    828       Magnesium or manganese 3 (By similarity).
FT   METAL       840    840       Magnesium or manganese 3 (By similarity).
FT   METAL       840    840       Magnesium or manganese 4 (By similarity).
FT   METAL       842    842       Magnesium or manganese 4 (By similarity).
SQ   SEQUENCE   1076 AA;  117613 MW;  6ECA5918A9CB0500 CRC64;
     MPKRTDIQSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPDM
     ADATYIEPIQ WEVVRKIIEK ERPDAVLPTM GGQTALNCAL DLEKHGVLAE FGVEMIGATA
     DAIDKAEDRS RFDKAMKSIG LECPTADTAK TMEEAYKVLD MVGFPCIIRP SFTMGGTGGG
     IAYNKEEFEE ICRRGLDLSP TNELLIDESL IGWKEYEMEV VRDKNDNCII VCAIENFDPM
     GIHTGDSITV APAQTLTDKE YQLMRNASLA VLREIGVETG GSNVQFGINP KDGRMVIIEM
     NPRVSRSSAL ASKATGFPIA KVAAKLAVGF TLDELMNDIT GGATPASFEP TIDYVVTKIP
     RFNFEKFAGA NDRLTTQMKS VGEVMAIGRN QQESLQKALR GLEVGANGFD EMVDLDSPDA
     LSKIRHELKE AGAERIWYIA DAFRAGLSVD GVFNLTQIDR WFLVQIEDLV KTEEVVKAGG
     FAGLTEDLLR KLKRKGFADT RLSKLLGVAE SEIRRLRDQF DIHPVYKRVD TCAAEFSSDT
     AYMYSSYDDE CEANPTDKDK IMILGGGPNR IGQGIEFDYC CVHASLALRE DGYETIMVNC
     NPETVSTDYD TSDRLYFEPV TLEDVLAIAR VEKPKGVIVQ YGGQTPLKLA RALEAAGVPI
     IGTSPDAIDR AEDRERFQVA VDRLGLLQPQ NVTVTTMEQA VEKSREIGFP LVVRPSYVLG
     GRAMEIVYDE QDLRRYFNEA VSVSNESPVL LDSFLDDAVE VDVDAICDGE RVVIGGIMEH
     IEQAGVHSGD SACSLPAYTL SQEIQDVMRE QVEKLAFELG VRGLMNTQFA VKDNEVYLIE
     VNPRAARTVP FVSKATGAPL AKIAARVMAG QSLEKQGFTK EIIPPYYSVK EVVLPFNKFP
     GVDPLLGPEM RSTGEVMGVG ATFAEAYAKA ELGCGSVYPE GGRALLSVRE GDKQRVVDLA
     SKLVKLGYQL DATHGTAVIL GEAGINPRLV NKVHEGRPHI LDRIKNNEYT YIVNTAAGRQ
     AIEDSKVLRR GALAEKVNYT TTLNAAFATC MAQTADAKSS VTSVQELHAK VKASQA
//