CARB_ZYMMO
ID CARB_ZYMMO Reviewed; 1112 AA.
AC O50236; Q5NM19;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 125.
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=ZMO1617;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Lee J.S., Jin S.J., Kang H.L., Kang H.S.;
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AE008692; Type=Frameshift; Evidence={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; AF086791; AAC70356.1; -; Genomic_DNA.
DR EMBL; AE008692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T33717; T33717.
DR AlphaFoldDB; O50236; -.
DR SMR; O50236; -.
DR PRIDE; O50236; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001173; 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; 3.40.50.1380; -; 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; 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..1112
FT /note="Carbamoyl-phosphate synthase large chain"
FT /id="PRO_0000145070"
FT DOMAIN 133..330
FT /note="ATP-grasp 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 716..907
FT /note="ATP-grasp 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT DOMAIN 973..1112
FT /note="MGS-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01202"
FT REGION 1..404
FT /note="Carboxyphosphate synthetic domain"
FT REGION 405..587
FT /note="Oligomerization domain"
FT REGION 588..972
FT /note="Carbamoyl phosphate synthetic domain"
FT REGION 973..1112
FT /note="Allosteric domain"
FT BINDING 159..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 742..799
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 866
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 878
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 878
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT BINDING 880
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT CONFLICT 163
FT /note="Missing (in Ref. 1; AAC70356)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..282
FT /note="Missing (in Ref. 1; AAC70356)"
FT /evidence="ECO:0000305"
FT CONFLICT 560..591
FT /note="CAAEFEAKTPYMYSTYEAPFFGEPVCDSLPSN -> ARLNLKPKRLICIPLM
FT KRLSLVNLFAILCQAI (in Ref. 1; AAC70356)"
FT /evidence="ECO:0000305"
FT CONFLICT 940..956
FT /note="Missing (in Ref. 1; AAC70356)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1112 AA; 119529 MW; B65A11546F8E085D CRC64;
MPKRTDLQSI MIIGAGPIVI GQACEFDYSG TQACKALREE GYRVILVNSN PATIMTDPDM
ADATYIEPIT PEVVARIIEK ERPDALLPTM GGQTALNTAL ALASDGTLEK FNCEMIGADA
TAIDKAEDRL KFRQAMDKIG LESPRSSVAH SLEEALDGLD YVGLPAIIRP SFTMGGTGGG
VAYNKEEFID IVSGGLSASP TQEVLIEESV IGWKEYEMEV VRDRHDNCII ICSIENIDPM
GVHTGDSITV APALTMTDKE YQIMRNASIA VLREIGVETG NGGSNVQFAL NPENGRLVVI
EMNPRVSRSS ALASKATGFP IAKVATKLAI GYTLDEITND ITGATPASFE PTIDYVVTKI
PRFAFEKFKN AKPLLTTAMK SVGEVMAIGR SFPESLQKAL RGLENGLSGL DPVEALVGAN
PSVIEAELAR PTPDRLLVAA QALREGLPAE KICEITHYDP WFIARLAEII AAENEVISNG
LPLEAAAFRR LKAMGFSDKR LADLALQSAH LRGLGKAQAK GSGIVHDALQ AMTGGVTEAE
VRTLRHSLNI RPVFKRIDSC AAEFEAKTPY MYSTYEAPFF GEPVCDSLPS NRKKVVILGG
GPNRIGQGLE FDYCCCHACF ALEAAGYETI MVNCNPETVS TDYDTSDRLY FEPLTGEDVL
EILHTEQKNG TLVGVIVQFG GQTPLKLAAE IEKAGIPILG TSPDAIDLAE DRERFSALVS
ELGLLQPANG IARSRDEAIS VADKIGYPIL IRPSYVLGGR AMEIIDGPSQ LDDYIHTAVK
VSGESPVLID QYLRDATEVD VDAVADGDDV VVAGILQHIE EAGIHSGDSA CSIPPYSLPA
SIIEEIKSQT DKLARALKVQ GLMNIQFAVK GDKVYLIEVN PRASRTVPFV AKADGRPVAQ
VAARVMAGEK LRNLPEISWP EGYTAVKEAV FPWARFPGVD PVLSPEMKST GEVMGIDIDF
PMAFAKAQLA AGNALPRAGT FFISVKDSDK AQIVEPIKAL TDLGIKLVAT DGTARYLQSK
GVPVERVNKV REGRPHIVDL IKDGAISLVV NTTEGWQSLQ DSASIRSSVV LAPVPYFTTA
AAAIVAAEAI VAIKARELEV RSLQSYHSMK HA
