ID A0A285NV21_9AQUI Unreviewed; 532 AA.
AC A0A285NV21;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SNZ13320.1};
GN ORFNames=SAMN06265353_0698 {ECO:0000313|EMBL:SNZ13320.1};
OS Hydrogenobacter hydrogenophilus.
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobacter.
OX NCBI_TaxID=35835 {ECO:0000313|EMBL:SNZ13320.1, ECO:0000313|Proteomes:UP000218627};
RN [1] {ECO:0000313|EMBL:SNZ13320.1, ECO:0000313|Proteomes:UP000218627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2913 {ECO:0000313|EMBL:SNZ13320.1,
RC ECO:0000313|Proteomes:UP000218627};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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; OBEN01000002; SNZ13320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285NV21; -.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000218627; 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 CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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 PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
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}.
FT DOMAIN 121..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 395..532
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 532 AA; 59214 MW; 5E3D5B8FB55CE389 CRC64;
MKKVLILGSG PNRIGQGIEF DYACVHAIYA LREEGIETIM INCNPETVST DYDTADKLYF
EPIVLENVLE VIRREKPDGV FLQFGGQTPL KLSLPLKKAN INILGIQPES IDIAEDRELF
KQLIDRLGIK QPPSSAVRSK QEALKVAESI GYPVLVRPSY VLGGRAMRIV YDEEELISYL
EEAVSVSYER PILIDKYLSD SVEVDVDAIG DGEDYLIGAV MEHIEEAGIH SGDSAACIPP
YTLKEEVINA IKEQSKKIAK ALSVKGLINL QFAVKNDEVF VLEVNPRASR TVPFVSKTIG
YPLAKLAAKI GVGRKLRQLV PEVFDRIRKG DVHIASDFMS ANKKLYAVKE VVFPWKRFPE
VDPLLGPEMK STGEVMAIDE EFGMAYYKAQ LAVGNRLPTK GRVFISVADR DKEKVIDLAK
GFKKIGFEVC ATAGTHKFLK EHGIDTIHVL KVSEGRPHVV DMITNGEINL VINTPTGKKE
RSDAYYIRRA VVQYDVPYTT TVRGGYAILS AIECFIKEGG KLRVYALQDL YL
//
