CARB_METHJ
ID CARB_METHJ Reviewed; 1056 AA.
AC Q2FLD9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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}; OrderedLocusNames=Mhun_0115;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_01210}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000255|HAMAP-
CC 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 the
CC 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}.
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DR EMBL; CP000254; ABD39893.1; -; Genomic_DNA.
DR RefSeq; WP_011447189.1; NC_007796.1.
DR AlphaFoldDB; Q2FLD9; -.
DR SMR; Q2FLD9; -.
DR STRING; 323259.Mhun_0115; -.
DR EnsemblBacteria; ABD39893; ABD39893; Mhun_0115.
DR GeneID; 3923734; -.
DR KEGG; mhu:Mhun_0115; -.
DR eggNOG; arCOG01594; Archaea.
DR HOGENOM; CLU_000513_1_0_2; -.
DR OMA; IEPAGIH; -.
DR OrthoDB; 911at2157; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001941; 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; 1.
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 Pyrimidine biosynthesis; Reference proteome; Repeat.
FT CHAIN 1..1056
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_1000066364"
FT DOMAIN 131..324
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 663..854
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 920..1056
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..398
FT /note="Carboxyphosphate synthetic domain"
FT REGION 399..532
FT /note="Oligomerization domain"
FT REGION 533..921
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 922..1056
FT /note="Allosteric domain"
FT BINDING 157..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 689..746
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 813
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 825
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 825
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 827
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ SEQUENCE 1056 AA; 115575 MW; 2061C94ECE706E5B CRC64;
MPRDPSIKKV LLIGSGPIQI GQAAEFDFSG SQACRALREE GVSVVLVNSN PATIQTDPDM
ADVTYVEPLQ ADIIAKIIKK EKPDGILSGM GGQTGLNLTA ELAEMGALEG VKILGTPLKA
IYEGEDREKF RDLMNRIGEP VPRSVIVSSL DQLEHAASVV GFPAIIRPAY TLGGAGGGIA
YNLDELRRIV ELGLGKSRIH QVLIEESVAG WKEIEFEVMR DANDTCITIC GMENVDPMGV
HTGESVVVAP ILTLRDDEFH LLRNAALKII RALDVQGGCN IQFAFKGDDE YRVIEVNPRV
SRSSALASKA TGYPIARVAS KIAIGLRLDE ILNTVTGKTP ASFEPSIDYV VVKVPRWPFD
KFKTADRTLT TAMKSTGEVM AIGRCVEEAF LKALRSLDTD VEHHTVLSEL KMILSRPTDE
RFGALFDALR QGMTLNEIAE ITRITPFWLE KIQNIVEMEK ALTAHPDDAT ILKAKEFGFS
DLEIAQYSGK DVSEVESKVG LPVYKMVDTC AAEFPAQTPY FYSTYGDKVC EVTHSDRKKV
MILGSGPIRI GQGIEFDYCT VHAVTALRED GYEVHVVNNN PETVSTDFDT SDRLFFEPMT
LEDVSHILQK DDYYGVMVQF GGQNAVNLAV PLKNEIDRLN LKTRILGTTP DAMDMAEDRD
RFSVLLDSLS IPTPPNGSAY SEQEAYATAE RIGYPVLVRP SYVLGGRAME IVHDDTELAT
YMREAVRVSK SHPVLIDRFL QNAIELDVDA VCDGTDVIIG GIMEHIETAG VHSGDSACVI
PPQSLSPEIL ADVRDYTRKI ALGLGVVGLV NIQFAVQGST VYVLEANPRA SRTVPFVAKS
VGIPLAKIAA RVMMGERLAD MPYKEIEVSH VAVKEVLLPF NKLPGVDTVL GPEMKSTGEV
MGIDYDFGRA YYKASIAAHN RLPKSGNVFI SVTDDLKDQI LQVAKTFTEN GLSIYATSGT
VEFFAERGIT ANLVRKIAEG SPNVLDMLRA GEISLIINNF ADKQSRHDHQ QIMRVAVDYG
TPYITTLQAA VAAAEAINSV REENLTIEPL QHYIGR
