ID   A0A4D6XVC8_9GAMM        Unreviewed;      1079 AA.
AC   A0A4D6XVC8;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-SEP-2019, entry version 2.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000256|HAMAP-Rule:MF_01210};
GN   ORFNames=D9V61_00720 {ECO:0000313|EMBL:QCI17551.1};
OS   Buchnera aphidicola (Acyrthosiphon lactucae).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=1241832 {ECO:0000313|EMBL:QCI17551.1};
RN   [1] {ECO:0000313|EMBL:QCI17551.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ala {ECO:0000313|EMBL:QCI17551.1};
RA   Chong R.A.;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QCI17551.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Ala {ECO:0000313|EMBL:QCI17551.1};
RA   Moran N.A.;
RT   "Genome evolution of the obligate endosymbiont Buchnera aphidicola.";
RL   Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC         Rule:MF_01210, ECO:0000256|SAAS:SAAS01124510};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00981842};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00611658};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00981844}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS01000080}.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00570548}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01210, ECO:0000256|SAAS:SAAS00570556}.
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DR   EMBL; CP034891; QCI17551.1; -; Genomic_DNA.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
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_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; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981831};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981841};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710217};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00710245, ECO:0000313|EMBL:QCI17551.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00981805};
KW   Manganese {ECO:0000256|SAAS:SAAS00459951};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00086100};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710285};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS01000143};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981845}.
FT   DOMAIN      133    328       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      679    870       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION        1    403       Carboxyphosphate synthetic domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      404    553       Oligomerization domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      554    936       Carbamoyl phosphate synthetic domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      937   1079       Allosteric domain. {ECO:0000256|HAMAP-
FT                                Rule:MF_01210}.
SQ   SEQUENCE   1079 AA;  120621 MW;  AE9B5B2D38E71B29 CRC64;
     MPKSTDIKSI LILGAGPIVI GQACEFDYSG AQACKALKEE GYKIILVNSN PATIMTDPCM
     ADSTYIEPIH WKIVEKIIQK EKPDALLPTM GGQTALNCAL KLDQKGVLKT HGVKIIGATV
     NAIKKAENRK LFEHSMKKLN LETAKCGIAH NIQEAFLVLN DVGFPCIIRP SFTMGGHGGG
     IAYNHEEFEK ICERGLKLSP NTELLIDESL IGWKEYEMEV VRDRNDNCII VCSIENLDPM
     GIHTGDSITV APAQTLTDKE YQVMRNASMA ILREIGVETG GSNVQFAINP KNGRMIVIEM
     NPRVSRSSAL ASKATGFPIA KIAAKLAIGY TLDELTNDIT GMNTTASFEP SIDYIVTKIP
     RFNFEKFPGC DDRLTTQMKS VGEVMAIGRT FQESIQKAIR GLELGVSGFD SKISHLDPEY
     LIKIRRELKD AGSERIWYIG DAFRSGMSVN DVFNLTSIDP WFLVQIEEII QLENKIIKNG
     FLGLKYDFFY LIKRKGFSDQ RIAILTQKNE SQIRELRYKL NLHPVYKRID TCSAEFSTET
     AYMYSTWEDE CESYPNKNNK KIIILGGGPN RIGQGIEFDY CCVHAAQALR EDGFEAIMIN
     CNPETVSTDY DISDRLYFEP ITLENVLEIV RIEKPRGIII QYGGQTPLKL AREFEKEGVP
     IIGTSPDSID KAEDRDRFQK IVTKLKLQQP LNATVLTLDE AYKQAEIIGY PIMVRPSYVL
     GGRAMEIVYE QYGLKNYFKT VLKENNTTPI LLDQYLNYAT EVDVDAVCDG KTVLIGGIME
     HIEQAGVHSG DSACSLPVYT LTNKVQNEIR KQVTKLAFEL SVKGLMNVQF AIKRNIIYII
     EVNPRAARTV PFISKATGLA LAKISARVMY GKTLLEQGFI KEIIPPYFSV KEAVLPFDKF
     QGVDPILGPE MRSTGEVMGM GKNFSEAFSK AMLGAHTNMK KSGRILLSVR DDDKNNIVNL
     AVKLKKIGFK IDATKGTSIA LRKSGISSRL VNKVHEGRPH IQDRLKNGEY SYIVNTTSSH
     QGIKDSKLIC RSALQYKVHY DTTVNGAFAT VMALNENPIK NIKSLQEMHK KIKLFYKKK
//