ID   I2SLM0_ECOLX            Unreviewed;      1073 AA.
AC   I2SLM0;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   05-SEP-2012, entry version 2.
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=EC12264_0032;
OS   Escherichia coli 1.2264.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=869675;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=1.2264;
RA   Brinkac L., Radune D., Sanka R., Selengut J., DebRoy C., Feng P.,
RA   Fratamico P.M., Kapur V., Kariyawasam S., Losada L., Nierman W.C.,
RA   Nelson K.;
RL   Submitted (DEC-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; AEZO02000031; EIH21691.1; -; Genomic_DNA.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:EC.
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      679    870       ATP-grasp 2 (By similarity).
FT   NP_BIND     159    216       ATP (By similarity).
FT   NP_BIND     705    762       ATP (By similarity).
FT   REGION        1    403       Carboxyphosphate synthetic domain (By
FT                                similarity).
FT   REGION      404    553       Oligomerization domain (By similarity).
FT   REGION      554    936       Carbamoyl phosphate synthetic domain (By
FT                                similarity).
FT   REGION      937   1073       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       829    829       Magnesium or manganese 3 (By similarity).
FT   METAL       841    841       Magnesium or manganese 3 (By similarity).
FT   METAL       841    841       Magnesium or manganese 4 (By similarity).
FT   METAL       843    843       Magnesium or manganese 4 (By similarity).
SQ   SEQUENCE   1073 AA;  117870 MW;  A9B02AF34675026B CRC64;
     MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM
     ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA
     DAIDKAEDRR RFDVAMKKIG LETARSGIAH TMEEALAVAA DVGFPCIIRP SFTMGGSGGG
     IAYNREEFEE ICARGLDLSP TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM
     GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM
     NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP
     RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA
     LTKIRRELKD AGAERIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG
     ITGLNAEFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT
     AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN
     CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP
     VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM AVEKAKEIGY PLVVRPSYVL
     GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG EMVLIGGIME
     HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI
     EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF
     PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR EGDKERVVDL
     AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTSGR
     RAIEDSRVIR RSALQYKVHY DTTLNGGFAT AMALNADATE KVISVQEMHA QIK
//