ID A0A1M6QNS8_9BACT Unreviewed; 1072 AA.
AC A0A1M6QNS8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SHK21798.1};
GN ORFNames=SAMN05720762_10197 {ECO:0000313|EMBL:SHK21798.1};
OS Fibrobacter sp. UWH4.
OC Bacteria; Fibrobacterota; Fibrobacteria; Fibrobacterales; Fibrobacteraceae;
OC Fibrobacter.
OX NCBI_TaxID=1896210 {ECO:0000313|EMBL:SHK21798.1, ECO:0000313|Proteomes:UP000184331};
RN [1] {ECO:0000313|EMBL:SHK21798.1, ECO:0000313|Proteomes:UP000184331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWH4 {ECO:0000313|EMBL:SHK21798.1,
RC ECO:0000313|Proteomes:UP000184331};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FRAY01000001; SHK21798.1; -; Genomic_DNA.
DR RefSeq; WP_072976489.1; NZ_FRAY01000001.1.
DR AlphaFoldDB; A0A1M6QNS8; -.
DR STRING; 1896210.SAMN05720762_10197; -.
DR OrthoDB; 9804197at2; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000184331; 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; -; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 2.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 132..326
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 671..863
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 929..1072
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1072 AA; 117969 MW; 09D323F441C95D27 CRC64;
MKIEGIDKVL IIGSGPIVIG QACEFDYSGT QACKALREQG YKIVLVNSNP ATIMTDPVMA
DATYIEPLNV ARLTQIIEKE RPQALLPNLG GQTGLNLASA LSKAGVLDKY GVKVIGVNLD
AIERGEDREI FKETMQKLGI DTPRSGICHS VEEAEKIVAE IGYPVVVRPA YTMGGAGGGF
CYNVEELRTI CSNGLELSMT HQCLIEESIL GWEELEVEVV RDSKNQMIAI CFIENIDPVG
VHTGDSFCAA PFLTIDKKLE EELKEKAFKI VESIGVIGGT NVQFAHDPKT GRVVIIEINP
RTSRSSALAS KATGFPIALI SAKLAAGLTL DQIPYWRDGS LEKYTPSGDY VVLKFARWAF
EKFRGVDDCL GTQMKAVGEV MAIGKTYKET LQKAIRGLEN GRSGLGFAKD FNKKSKEELL
EMLKTPSSER HFQMYEAIRK GATDEEIFAA TYEKAYFVQQ MRELVELEEE MLKTPGRLPS
DELLIKAKKD GFSDKYIAKI LGIREKDVRK KRTELGVVEG WCAVPVSGVE NQFYYYSTYN
CKDESTASTN PKKIMILGGG PNRIGQGIEF DYCCCHAAMA LREMGYETIM VNCNPETVST
DYDTSDKLYF EPVSLEDVLQ IYHKEKPAGV IVQFGGQTPL NIARALSDEG VKILGTSIDS
IDIAEDRDLF RKMMDQLGIP MPESGMATNI DEALACVKQI GGYPVMIRPS FVLGGRGMEV
IYDENMLREY VAKAVGVTPD RPLLIDRFLH NALECEADAL SDGEHVYIPS VMEHVELAGV
HSGDSACIIP PVTITKENLA TIKDYTRKIA EALHVCGLMN MQYAIEDGKV FVLEANPRAS
RTVPLVSKVC NTQMARLATR LMLGAKLEDL KLKDKKFNHH GAKEAVFPFD KFPKVDPVLG
PEMRSTGEVL GLSDDYALAY YKSQEAAGSF LPNEGAVLIS LSDKVNLSEQ AIEIGKEFQK
LGFKIYATEG TAKFYEAAGV KCEVVNKIAE GRPNVLDIIL NKQVNLIINT PWAKRDAIKD
ESAIRKAAIK YKVPYITTLA GAYNTVKGIA AARNGHGAVK SLQEYHASIE EV
//
