ID L0FVL2_ECHVK Unreviewed; 939 AA.
AC L0FVL2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:AGA77043.1};
GN OrderedLocusNames=Echvi_0768 {ECO:0000313|EMBL:AGA77043.1};
OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Echinicola.
OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA77043.1, ECO:0000313|Proteomes:UP000010796};
RN [1] {ECO:0000313|Proteomes:UP000010796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC {ECO:0000313|Proteomes:UP000010796};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Echinicola vietnamensis DSM 17526.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; CP003346; AGA77043.1; -; Genomic_DNA.
DR RefSeq; WP_015264609.1; NC_019904.1.
DR AlphaFoldDB; L0FVL2; -.
DR STRING; 926556.Echvi_0768; -.
DR KEGG; evi:Echvi_0768; -.
DR PATRIC; fig|926556.3.peg.770; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_10; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000010796; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:UniProt.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 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; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM01209; GARS_A; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000010796};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 134..329
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 677..868
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 939 AA; 104691 MW; 05C0245414D5BEC2 CRC64;
MPKDNSIKHV LIIGSGPIVI GQACEFDYSG SQAARSLREE GITVTLINSN PATIMTDPVT
ADNVYLLPLE KKSLVKILEE HPDIDCVLPT MGGQTALNLA IEADKAGIWD RFKVRMIGVD
IDAIETAENR EKFKALLEEL NVGVCIGKTA TSFLQGKEIA QEIGFPLVIR PSYTLGGTGG
GFVEKEEEFE NALMSGLKAS PTHEVLIEQS ILGWKEYELE VLRDSLGNMV VICSIENFDP
MGVHTGDSIT VAPAMTLPDT VYQEMRNLAI KMMNGIGNFA GGCNVQFSVS PDNQTIIGIE
INPRVSRSSA LASKATGYPI AKVAAKLAIG YNLDELKNSI TGSTSAFFEP AIDYVIVKIP
RWNFDKFKGS DRRLGLSMKA VGEVMGIGGN FQEALQKACQ SLEIKRNGLG ADGKELKNQE
QILYSLEHPS WNRLFHIYDA FKLGISFRTI HDLTKIDKWF LKQIEELVHL DITLDKYTLD
TIPKDLMMLA KHKGYADRQI AHLLGCLESE VFNKRRDEMG IKRVYKLVDT CAAEFEAQTP
YYYSSFGEEN ESQVSDRKKV IVLGSGPNRV GQGIEFDYSC VHGVLAAKEC GYETIMINCN
PETVSTDFDI ADKLYFEPVF WEHIYEIILH EKPEGVIVQL GGQTALKLAE KLEKYGIKIL
GTSFEALDLA EDRGEFSSLL KENDVPYPEF GTIHSTDEAL ELCKTIGFPL LVRPSYVLGG
QGMKIVINEK ELEQHVVEVL KDIPDNEILL DHFLEGAIEA EADAICDGEN VYIIGIMQHI
EPAGIHSGDS YAVLPPYNLG DLVVRQIETF TEKIALALKT KGLINIQFAV KDDKVYVIEA
NPRASRTVPF ICKAYKEPYV NYAVKVMLGE NKVTDFEFKP YKKGYAIKEP VFSFHKFPNV
NKELGPEMKS TGEAIYFIDD LMDDYFLKIY SERNLYLSR
//
