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CARB_FUSNN
ID   CARB_FUSNN              Reviewed;        1058 AA.
AC   Q8RG86;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 127.
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=FN0422;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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=AAL94625.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE009951; AAL94625.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_603326.2; NC_003454.1.
DR   AlphaFoldDB; Q8RG86; -.
DR   SMR; Q8RG86; -.
DR   STRING; 190304.FN0422; -.
DR   EnsemblBacteria; AAL94625; AAL94625; FN0422.
DR   KEGG; fnu:FN0422; -.
DR   PATRIC; fig|190304.8.peg.999; -.
DR   eggNOG; COG0458; Bacteria.
DR   HOGENOM; CLU_000513_1_0_0; -.
DR   InParanoid; Q8RG86; -.
DR   OMA; IEPAGIH; -.
DR   BioCyc; FNUC190304:G1FZS-1016-MON; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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   Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Ligase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome; Repeat.
FT   CHAIN           1..1058
FT                   /note="Carbamoyl-phosphate synthase large chain"
FT                   /id="PRO_0000145007"
FT   DOMAIN          133..327
FT                   /note="ATP-grasp 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          671..861
FT                   /note="ATP-grasp 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   DOMAIN          930..1058
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..1058
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         284
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         697..754
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         820
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         832
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         832
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
FT   BINDING         834
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01210"
SQ   SEQUENCE   1058 AA;  117452 MW;  ED7037AF77C1E39F CRC64;
     MPKRKDIKTI LVIGSGPIII GQAAEFDYAG TQACLSLREE GYEVILVNSN PATIMTDKEI
     ADKVYIEPLT VEFLSKIIRK EKPDALLPTL GGQVALNLAV SLHESGILDE CGVEILGTKL
     TSIKQAEDRE LFRDLMNELN EPVPDSAIVH TLEEAENFVK EIDYPVIVRP AFTMGGTGGG
     ICYNEEDLHE IVPNGLNYSP VHQCLLEKSI AGYKEIEYEV MRDSNDTAIV VCNMENIDPV
     GIHTGDSIVV APSQTLTDRE HHMLRDVSLK IIRALKIEGG CNVQIALDPN SFKYYIIEVN
     PRVSRSSALA SKATGYPIAK IAAKIAVGMT LDEIINPVTK SSYACFEPAI DYVVTKIPRF
     PFDKFGDGDR YLGTQMKATG EVMAIGRTLE ESLLKAIRSL EYGVHHLGLP NGEEFSLEKI
     IKRIKLAGDE RLFFIGEALR RDVSIEEIHE YTKIDLFFLN KMKNIIDLEH LLKDNKGNIE
     LLRKVKTFGF SDRVIAHRWE MTEPEITELR HKHNIRPVYK MVDTCAAEFD SNTPYFYSTY
     EFENESTRSD KEKIVVLGSG PIRIGQGIEF DYATVHAIMA IKKLGYEAIV INNNPETVST
     DFSISDKLYF EPLTQEDVME ILDLEKPLGV VVQFGGQTAI NLADKLVKNG IQILGSSLDS
     IDTAEDRDRF EKLLIGLKIP QPLGKTAFDV ETALKNANEI GYPVLVRPSY VLGGRAMEIV
     YNDEDLTKYM EKAVHINPDH PVLIDRYLIG KEIEVDAISD GENTFIPGIM EHIERAGVHS
     GDSISIYPPQ SLSEKEIETL IDYTKKLASG LEVKGLINIQ YVVSKGEIYV LEVNPRASRT
     VPFLSKVTGV PVANIAMQCI LGKKLKDLGF TKDIADIGNF VSVKVPVFSF QKLKNVDTTL
     GPEMKSTGEV IGTDVNLQKA LYKGLTAAGI KIKDYGRVLF TIDDKNKEAA LNLAKGFSDV
     GFSILTTEGT GIYFEEYGLK VKKVGKIDNS DYSVLDAIQN GDVDIVINTT TKGKSSEKDG
     FRIRRKATEY GVICFTSLDT ANALLRVIES MSFRVQTL
 
 
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