ID A0A1X7L9L5_9SPHI Unreviewed; 939 AA.
AC A0A1X7L9L5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Carbamoyl-phosphate synthase large subunit {ECO:0000313|EMBL:SMG50174.1};
DE EC=6.3.5.5 {ECO:0000313|EMBL:QBQ42424.1};
GN Name=carB {ECO:0000313|EMBL:QBQ42424.1};
GN ORFNames=E2P86_15215 {ECO:0000313|EMBL:QBQ42424.1}, SAMN05660862_3752
GN {ECO:0000313|EMBL:SMG50174.1};
OS Sphingobacterium psychroaquaticum.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=561061 {ECO:0000313|EMBL:SMG50174.1, ECO:0000313|Proteomes:UP000192980};
RN [1] {ECO:0000313|EMBL:SMG50174.1, ECO:0000313|Proteomes:UP000192980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22418 {ECO:0000313|EMBL:SMG50174.1,
RC ECO:0000313|Proteomes:UP000192980};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QBQ42424.1, ECO:0000313|Proteomes:UP000294378}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SJ-25 {ECO:0000313|EMBL:QBQ42424.1,
RC ECO:0000313|Proteomes:UP000294378};
RA Sun J.-Q., Xu L.;
RT "Completed genome sequence and physiology data of Sphingobacterium
RT psychroaquaticum strain SJ-25 isolated from farm land soil.";
RL Submitted (MAR-2019) 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; CP038029; QBQ42424.1; -; Genomic_DNA.
DR EMBL; FXAU01000008; SMG50174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7L9L5; -.
DR STRING; 561061.SAMN05660862_3752; -.
DR KEGG; spsc:E2P86_15215; -.
DR OrthoDB; 9804197at2; -.
DR Proteomes; UP000192980; Unassembled WGS sequence.
DR Proteomes; UP000294378; 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; 1.
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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:QBQ42424.1};
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:UP000192980};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 133..328
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 676..867
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 939 AA; 104455 MW; 4B2B89C5DFCC99C0 CRC64;
MPRNTSINSV LIIGSGPIVI GQACEFDYSG SQAALSLKEE GIKVSIINSN PATIMTDKVI
ADHVYLLPLT CESIEQILQE QQIDAVLPTM GGQTALNLCI EASELGLWEK YNVKVIGVDV
AAIEKTENRE AFRQLMVDIG VGVATSKIAN SFLEGKEAAQ EIGYPLVIRP SYTLAGTGGG
FVHRKEDFDA ALNRGLHASP THEVLVEQAV LGWKEFELEL LRDTNDNVII ICTIENFDPM
GIHTGDSITV APGMTLSDKC YQDMRNQAIR MMRSIGTFAG GCNVQFSVNP ENEEIIAIEI
NPRVSRSSAL ASKATGYPIA KIAAKLAIGY NLDELQNQIT KTTSAYFEPT LDYVIVKIPR
FNFDKFKGAN KELGLQMKAV GEVMAIGRTF IEALQKACQS LETNRWGLGA DGRQLRNLED
IMESLEHPSG DRIFHIKDAF ELGVPLESIR KATLIDKWFL VQIQELVHLE TELRRYQLNN
IPRDFFMTLK QKGYSDAQIS WLLGNVSEDE VYDRRKELGI NRVYKMVDTC AAEFPAQTPY
YYSTFEDENE SIVSDKKKIV VLGSGPNRIG QGIEFDYSCV HGLLAAKECG YEAIMINCNP
ETVSTDFNMA DKLYFEPVFW EHVREIIELE KPEGVIVQLG GQTALKMAKQ LEALGIKIIG
TSFENMDLAE DRGRFSDLLK DLDIPYPQYG VATSAEEALV VANRVGYPVL VRPSYVLGGQ
GMSIVINDED LEKAVVNLLK TLPGNQILID HFLDRAEESE SDSICDGDDV HIIGMMEHIE
PAGIHSGDSS AVLPPFSLSE NVQKKMEEYS VKLAKALNVK GLLNIQFAVK DENVFVIEAN
PRASRTVPFI AKAYDVPYIK IATKIMLGEN KLKDFNIERK LTGWAIKEPV FSFSKFPEVD
KQLGPEMKST GEAIRFIKDL HDPYFRELVA KKSMFLNAQ
//
