ID V6HY89_9LEPT Unreviewed; 901 AA.
AC V6HY89;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:EQA62017.1};
GN Name=carB {ECO:0000313|EMBL:EQA62017.1};
GN ORFNames=LEP1GSC062_2003 {ECO:0000313|EMBL:EQA62017.1};
OS Leptospira alexanderi serovar Manhao 3 str. L 60.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049759 {ECO:0000313|EMBL:EQA62017.1, ECO:0000313|Proteomes:UP000018747};
RN [1] {ECO:0000313|EMBL:EQA62017.1, ECO:0000313|Proteomes:UP000018747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L 60 {ECO:0000313|EMBL:EQA62017.1,
RC ECO:0000313|Proteomes:UP000018747};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
RL Submitted (MAY-2013) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQA62017.1}.
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DR EMBL; AHMT02000040; EQA62017.1; -; Genomic_DNA.
DR AlphaFoldDB; V6HY89; -.
DR STRING; 100053.GCA_002009845_02914; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000018747; Unassembled WGS sequence.
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:0006520; P:amino acid metabolic process; IEA:UniProt.
DR CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 3.40.50.20; -; 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; 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; 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 {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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..123
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 502..693
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 760..901
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 901 AA; 101116 MW; 86DCABDFD7EBB9E2 CRC64;
MEESVLGWKE FELEVMRDLA DNVVIICSIE NIDPMGVHTG DSITVAPQQT LSDKEYQNLR
DMSIAIIREI GVETGGSNIQ FAVNPANGDV IVIEMNPRVS RSSALASKAT GFPIAKIAAL
LSIGYTLDEI KNDITRVTPA SFEPSIDYVV TKVPRFAFEK FPGTDDTLGV QMKAVGEAMA
IGRTFKESFQ KALRSLEIDR YGFGSDGYFQ ELLYARSLNS DQRKEWIDSF LKRPNDKRIF
YIKLAFDAEY TVDQIHDLCK VDRWFLWQME DLLKLEKEYS EKGDSVLAKM KRAGFSNRQL
SFLKNKKQIL DLLDGDLRVD LKKTEIQNIL KKSEEEIETK LGSEKILPVY KRIDTCAGEF
EAYTPYFYSS YDEEDESDVT STKSVMILGG GPNRIGQGIE FDYCCCQASY ALQELGVESI
MVNSNPETVS TDYDTSDRLY FEPLTLEDVY RIYQNEKPEG VIIQFGGQTP LKLARDLERK
GVKILGTSPD SIDRAEDRKR FVEVLEKLKL CSPESGIATS MEEAREIAQK VKYPILVRPS
YVLGGRAMLI INEEKELDRY MEKAEEISKD RPLLIDSFLE DAVEVDVDAL CDGKEVFVTG
IMEHIEEAGV HSGDSACILP PQTLSKNMMD EIRKATVDLA LELQVKGLIN IQYAVKNEIL
YIIEVNPRAS RTVPFVSKAL GHPIVKYATR IIMGESLKSL PLPKEMAFSQ VSVKEVVLPF
NKFPGVDTIL GPEMRSTGEV MGIASTVGEA FLKSQYMAGD ELPSQGTVFV SINDKTKPEL
LSYIKDLSEL GFNLIATSGT HKFLSDNGIL SSKINKVYDG IFPTALDYIR ENKIHLIINT
PLSRVTRDDS FTIRQAAIRF KVPCLTTSNA AKALIKGMVE MKNRGFTIHS LQEIHTMPKV
L
//
