CARY_ALKHC
ID CARY_ALKHC Reviewed; 1047 AA.
AC Q9K8V7;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=carB; OrderedLocusNames=BH2895;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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;
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; carbamoyl
CC phosphate from bicarbonate: step 1/1.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000004; BAB06614.1; -; Genomic_DNA.
DR PIR; G84011; G84011.
DR RefSeq; WP_010899042.1; NC_002570.2.
DR AlphaFoldDB; Q9K8V7; -.
DR SMR; Q9K8V7; -.
DR STRING; 272558.10175517; -.
DR EnsemblBacteria; BAB06614; BAB06614; BAB06614.
DR KEGG; bha:BH2895; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_9; -.
DR OMA; TKMKATG; -.
DR OrthoDB; 48855at2; -.
DR UniPathway; UPA00068; UER00171.
DR Proteomes; UP000001258; 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:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1030.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 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; 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; IPR016185; PreATP-grasp_dom_sf.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SUPFAM; SSF48108; SSF48108; 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; Ligase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..1047
FT /note="Carbamoyl-phosphate synthase arginine-specific large
FT chain"
FT /id="PRO_0000144988"
FT DOMAIN 133..327
FT /note="ATP-grasp 1"
FT DOMAIN 676..865
FT /note="ATP-grasp 2"
FT DOMAIN 937..1047
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..401
FT /note="Carboxyphosphate synthetic domain"
FT REGION 402..549
FT /note="Oligomerization domain"
FT REGION 550..933
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 934..1047
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 702..758
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 824
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 836
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 836
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 838
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1047 AA; 115860 MW; 1AAA7676D583A311 CRC64;
MPKRTDIQSV LVIGSGPIVI GQAAEFDYAG AQACLALREE GIQVILVNNN PATVMTDEAC
ADVVYFEPLT VASVKNIIER ERPDGLLATL GGQTGLNLAM KLEEAGILEA YNVELLGTPM
ESIKKGEDRE AFRQLMHELH EPVPESEIVH SVAEAVDFAN TVGYPIIVRP AYTLGGAGGG
IAESEEALIR IVKGGLELSP IQQCLIEKSI AGFKEIEYEV MRDSNDTCIT VCNMENIDPV
GVHTGDSIVV APSQTLTDQE YQMLRSASLK IIRTLGIVGG CNIQFALDPD SKQYYLIEVN
PRVSRSSALA SKATGYPIAR MAAKLSLGYG LHELKNPVTE DTYASFEPSL DYVVVKFPRW
PFDKLVHVNR ELGTQMKATG EVMAIERNLE AGLQKAVRSL EIKTHGLSLP SLSQWEDSEL
WVIVKKADDR RFFAILELLR RGVTIEAIHE QTKIDRFFLT SFAKLMTLEK EIAGQSLDDI
TSDELSTYKK YGFSDEWLAS SWGVGLADVR HTRKALGVVP SYKMVDTCAA EFEAKTPYYY
SSWTGENDLL LPEKAKERVL IIGSGPIRIG QGIEFDYCSV HGAKSLRARN FEAIIINNNP
ETVSTDYETA DRLYFEPLAV EDVLNVIEVE NVDHVIVQLG GQTAIGLTKG LEEAGVSILG
TTQDVIDQLE DRERFYEFMR SVEVPHIPGK TAETKEELLK AAQSIGYPIL LRPSYVIGGQ
GMFIASNQEE LAAFCEDKNH SVTFPILVDA YYPGVEFEVD VLTDGSDIFI PGMFEHVEKA
GVHSGDSMAV TPPPTLEAKW KQQAINYTRQ IAKGMAYKGL FNIQFVLYDE ELYVIEVNPR
ASRTVPIFSK ATSLPLITYT IDVLFGKTIA ELGLSAGYRK ESPYYTVKAP VFSYQKLAGL
DPLLEAEMKS TGELIAISKD LPSAFRKAFA WGEEQTPALF RKKGSVFCQV DRAYDTEWQP
LLRQLKEKGY SVVTEEAMSF SEWLASEDAI CLVSVPAPGQ KTGKQNREEA LKQRVTVVSD
LATFEKMIEC LEVKDGEPFL LPDVVMN
