CARB_ALKHC
ID CARB_ALKHC Reviewed; 1062 AA.
AC Q9K9V9;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific large chain;
DE EC=6.3.5.5;
DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain;
GN Name=pyrAB; OrderedLocusNames=BH2536;
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: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (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 the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}.
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DR EMBL; BA000004; BAB06255.1; -; Genomic_DNA.
DR PIR; H83966; H83966.
DR RefSeq; WP_010898687.1; NC_002570.2.
DR AlphaFoldDB; Q9K9V9; -.
DR SMR; Q9K9V9; -.
DR STRING; 272558.10175156; -.
DR EnsemblBacteria; BAB06255; BAB06255; BAB06255.
DR KEGG; bha:BH2536; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_9; -.
DR OMA; IEPAGIH; -.
DR OrthoDB; 48855at2; -.
DR UniPathway; UPA00070; UER00115.
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: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; 3.30.1490.20; -; 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; 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; 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 ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..1062
FT /note="Carbamoyl-phosphate synthase pyrimidine-specific
FT large chain"
FT /id="PRO_0000144987"
FT DOMAIN 133..327
FT /note="ATP-grasp 1"
FT DOMAIN 671..861
FT /note="ATP-grasp 2"
FT DOMAIN 930..1062
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..401
FT /note="Carboxyphosphate synthetic domain"
FT REGION 402..546
FT /note="Oligomerization domain"
FT REGION 547..929
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 930..1062
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 697..754
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 820
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1062 AA; 117814 MW; 533DD62812EAA691 CRC64;
MGKREDIKKI LVIGSGPIVI GQAAEFDYAG TQACQALKEE GYEVILVNSN PATIMTDTTM
ADRVYIEPLT LEFVSRIIRM ERPDGILPTL GGQTGLNMAV ELDQAGILKE YNVELLGTKL
DSIQQAEDRD LFRALMKELN EPVPDSEIIH TLEEAYTFVE RVGYPIIVRP AYTLGGTGGG
LVYNEEDLVE IVTSGLKYSP VTQCLVEKSI AGFKEIEYEV MRDGKDHAIV VCNMENIDPV
GVHTGDSIVV APSQTLSDRE YQMLRNSSLK IIRALGIEGG CNVQFALDPD SFQYYIIEVN
PRVSRSSALA SKATGYPIAK IAAKIAVGYT LDELLNPITQ TTYASFEPAL DYVVSKIPRW
PFDKFEAANR SLGTQMKATG EVMAIGRNLE ESLLKAVRSL EAGVYHLDQP DVNDLDKESL
EKKLTKPDDE RLFALGEAIR RGYTIEELWA LTKIDRFFLR SFARIIQLET QLKENVGDLE
LLKEAKERGF SDMIIADLWG TSEQEVYELR MNHGLSPVYK MVDTCAAEFA SATPYFYGTY
EEENESERTD KKSILVLGSG PIRIGQGIEF DYATVHTVWA IKEAGYEAII VNNNPETVST
DFSTSDKLYF EPLTVEDVMH IVNLEQPEGV IVQFGGQTAI NLASELAARG VKIIGTALED
MDRAEDRDKF EQTLVELNIP QPLGDTATSI EEARQIAERI GYPVLVRPSY VLGGRAMEIV
YKEEELLNYM AHAVKVNPKH PVLIDRYLTG KELEVDAISD GENVYIPGIM EHIERAGVHS
GDSIAVYPPQ TVPESLKQKL IERTIELARG LRIVGLLNIQ FVWHKDDVYV LEVNPRSSRT
VPFLSKVTGV PMANVATKVM LGKTLPQLGY ETGYHPEAKE VSVKVPVFSF AKLRRVDITL
GPEMKSTGEV MGRDKTLEKA LYKGLIASGM SIPTHGSVLF TIADKDKQEA ISLAKRFYQI
GFSILATEGT AHILHEEGIP VTTVNKISDE KPHLLDVIRA GDAQFVINTL TRGKQPARDG
FRIRRESVEN GVVCLTSLDT AEALLRVLES ITFSAESMPV MQ
