ID I4BZS0_DESTA Unreviewed; 1066 AA.
AC I4BZS0;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:AFM22811.1};
GN OrderedLocusNames=Desti_0062 {ECO:0000313|EMBL:AFM22811.1};
OS Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1).
OC Bacteria; Thermodesulfobacteriota; Desulfomonilia; Desulfomonilales;
OC Desulfomonilaceae; Desulfomonile.
OX NCBI_TaxID=706587 {ECO:0000313|EMBL:AFM22811.1, ECO:0000313|Proteomes:UP000006055};
RN [1] {ECO:0000313|Proteomes:UP000006055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49306 / DSM 6799 / DCB-1
RC {ECO:0000313|Proteomes:UP000006055};
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., Zeytun A.,
RA Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Desulfomonile tiedjei DSM 6799.";
RL Submitted (JUN-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 -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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DR EMBL; CP003360; AFM22811.1; -; Genomic_DNA.
DR RefSeq; WP_014807970.1; NC_018025.1.
DR AlphaFoldDB; I4BZS0; -.
DR STRING; 706587.Desti_0062; -.
DR KEGG; dti:Desti_0062; -.
DR PATRIC; fig|706587.4.peg.64; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_7; -.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000006055; 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:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01424; MGS_CPS_II; 1.
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 Gene3D; 3.40.50.1380; Methylglyoxal synthase-like 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; 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 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 Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000006055};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..327
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 671..862
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 928..1066
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1066 AA; 117642 MW; B96F6F973C26F7E6 CRC64;
MPKRSDIKKV MIIGSGPIVI GQACEFDYSG TQACKALRSL GYEIILVNSN PATIMTDPGM
ADITYIEPLN LQTMTKIIEL ERPDALLPNL GGQSGLNLSS ELYRTGVLEK YGVKIIGVQA
DAIERGEDRI AFKETMNRLG IEMPRSDPAF SVEEAERIAD ELGYPVVIRP AYTMGGTGGG
LVYNVDELRI VASRGIAASL VGQILVEESV LGWEELELEV VRDAKNQMIT VCFIENVDAM
GVHTGDSFCT APMLTIDSSL QERLQKHSYD IVEAIQVIGG TNIQFAHDPK TGRVVVIEIN
PRTSRSSALA SKATGFPIAL ISAMLAGGLT LDEIPYWRDG TLDKYTPSGD YVVVKFARWA
FEKFSGAVDK LGTQMRAVGE VMSIGKTYKE AFHKAIRSLE TGRYGFGFVK DFHEKSLGEL
MALLNEPSSE RQFIMYEALR KGADVEILHK KTHIKSWFIQ QMKDLVDLEE QILRFKGKDI
PDALLERAKK DGFSDRYLAK LLETSEKEVR TKREALGIVE GWEPVPVSGV ENAAYYYSTY
NAPDRVESSS RPKIMVLGGG PNRIGQGIEF DYCCVHAAFA IRDAGYESIM VNCNPETVST
DYDTSDKLYF EPLTVEDVLS IYRKEKPEGV IVQFGGQTPL NIASELAEAG VRIIGTSPDI
IDLAEDRDRF RNMMRKLSIP QPESGMAGSL DEALAVAKSI GYPLMVRPSY VLGGRAMQVI
HDETTLTRYM DAAEEVSRER PILIDKFLEK AIEAEADAVA DGVDAFVPAV MEHIELAGIH
SGDSACVIPP ISIPPKHLET IYEYTRKIAM ELGVVGLMNI QYAIANDTVY ILEANPRASR
TVPLVSKVCN IPMARIATQL MLGKKLGQFS TTRKLISHYG VKEAVFPFNM FPEVDPVLGP
EMRSTGEVLG LADSFGLAFY KAQEATQVPL PSRGVVLVSV TENERPALLE VVRQFTELGF
KIKATAGTHQ YLQEHGAQSE CALKLHEGRP HIVDHITNKE IHLVINTPDG KISKDDDSYI
RKAAIRNKIP HITTIAAAFA AARGIRAINR TKADVKSIQR YHEEIK
//
