ID H8KSI1_SOLCM Unreviewed; 937 AA.
AC H8KSI1;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Carbamoyl-phosphate synthase, large subunit {ECO:0000313|EMBL:AFD08532.1};
GN OrderedLocusNames=Solca_3528 {ECO:0000313|EMBL:AFD08532.1};
OS Solitalea canadensis (strain ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB
OS 12057 / USAM 9D) (Flexibacter canadensis).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Solitalea.
OX NCBI_TaxID=929556 {ECO:0000313|EMBL:AFD08532.1, ECO:0000313|Proteomes:UP000007590};
RN [1] {ECO:0000313|Proteomes:UP000007590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29591 / DSM 3403 / NBRC 15130 / NCIMB 12057 / USAM 9D
RC {ECO:0000313|Proteomes:UP000007590};
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., Lu M.,
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., Spring S., Schroeder M., Kopitz M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Solitalea canadensis DSM 3403.";
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; CP003349; AFD08532.1; -; Genomic_DNA.
DR RefSeq; WP_014681755.1; NC_017770.1.
DR AlphaFoldDB; H8KSI1; -.
DR STRING; 929556.Solca_3528; -.
DR KEGG; scn:Solca_3528; -.
DR eggNOG; COG0458; Bacteria.
DR HOGENOM; CLU_000513_1_0_10; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000007590; 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:UP000007590};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 675..866
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 937 AA; 104070 MW; 7813B81B3F3A219A CRC64;
MPRNESIKSV LIIGSGPIII GQACEFDYSG SQAALSLKEE GISVSIINSN PATIMTDKVI
ADHVYLLPLN CESIEQILQE QKIDAVLPTM GGQTALNLAK EAEERGIWAK YGVKVIGVDV
AAIEKTENRE EFRQLMIDIG VGVAPSKIAN SFLEGKEAAQ EIGFPLVIRP SYTLGGSGGG
FVHKKEDFDS ALNRGLQASP THEVLVEKAV IGWKEYELEL LRDSNDNVII ICSIENFDPM
GIHTGDSITV APAMTLSDRC YQDMRNQAIK MMRAIGTFAG GCNVQFSVSP DDESIIAIEI
NPRVSRSSAL ASKATGYPIA KIAAKLAIGY NLDEIENQIT KTTSAYFEPS LDYVIVKVPR
FNFQKFKGAN KELGLQMKSV GEVMAIGRSF TEALQKACQS LEISRNGLGA DGKQLKDLDK
IMDSLEHPSW DRLFHIKDAL ALGVPVSSVQ KATKIDRWFL MQIQDLVHLE LEIKRYSLAN
LPKDLLITAK QKGYSDLQLA YLLGVDEDAI YYKRKELGIR RVYKMVDTCA AEFPAQTPYY
YSTYEGENES IPSDKKKIIV LGSGPNRIGQ GIEFDYSCVH GLLAAKEAGY ESIMVNCNPE
TVSTDFNMAD KLYFEPVFWE HVREIIDLEK PEGVIVQLGG QTALKMAELL HKNNIKIIGT
TFPDMDVAED RGRFSDLLKD LDIPYPRYGV AHSADEAIKV ASEVGYPVLV RPSYVLGGQG
MEIVINDEEL ERAVVKLLRH MPDNKILIDH FLDRAEESES DSICDGEDVH IVGLMEHIEP
AGIHSGDSSA VLPPFSLSEN VQNKMKEYTI KLAKALNVRG LLNIQFAIKD ENVYVIEANP
RASRTVPFIA KAYDVPYINI ATKVMLGVNK LKDFTIEEKL KGYAIKEPVF SFDKFPEVNK
ELGPEMKSTG EAIRFIKDLE DPYFRHLVKE KSMYLSK
//
