ID   A0A0P7BXW4_9BACT        Unreviewed;       947 AA.
AC   A0A0P7BXW4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:KPM49359.1};
GN   ORFNames=AFM12_01685 {ECO:0000313|EMBL:KPM49359.1};
OS   Jiulongibacter sediminis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Jiulongibacter.
OX   NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM49359.1, ECO:0000313|Proteomes:UP000050454};
RN   [1] {ECO:0000313|EMBL:KPM49359.1, ECO:0000313|Proteomes:UP000050454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN14-9 {ECO:0000313|EMBL:KPM49359.1,
RC   ECO:0000313|Proteomes:UP000050454};
RA   Liu Y., Du J., Shao Z.;
RT   "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL   Submitted (JUL-2015) 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}.
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:KPM49359.1}.
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DR   EMBL; LGTQ01000005; KPM49359.1; -; Genomic_DNA.
DR   RefSeq; WP_055143543.1; NZ_LGTQ01000005.1.
DR   AlphaFoldDB; A0A0P7BXW4; -.
DR   STRING; 1605367.AFM12_01685; -.
DR   PATRIC; fig|1605367.3.peg.1676; -.
DR   OrthoDB; 9804197at2; -.
DR   Proteomes; UP000050454; 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: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   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}; 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:UP000050454};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          138..333
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          685..876
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   947 AA;  105610 MW;  D2289765497C0F8A CRC64;
     MPKNTNLKSV LIIGSGPIII GQACEFDYSG SQAARSLREE GIEVALINSN PATIMTDPLN
     ADYVYLKPLE KKYIEEILQI HVDMGKPIDA VLPTMGGQTA LNLAIECDEA GIFEKFNTKM
     IGVDINAIET TEDREKFRLK MKEIGVSVCE GRTAKSFLEG KEIAQEIGFP LVIRPSFTMG
     GYGGGFVNSP EEFDRALNAG LHASPVHEVL IEQSILGWKE YELELLRDNV GNIVIICTIE
     NFDAMGVHTG DSITVAPAMT LPDTIYQRMR DMAIKMMNGI GQFAGGCNVQ FALSPDDDTI
     IGIEINPRVS RSSALASKAT GYPIAKIAAK MAIGYNLDEL INPITGSTSA MFEPAIDYVI
     VKVPRWNFAK FKGADQKLGL QMKAVGEAMG IGRNFQEALQ KACQSLEIGR NGLGADGKEL
     KDQAALKESL EHPSWDRMFH IYDAFKAGLS FNTIQNLSKI DKWFLHQIEE LIHLEKEIMK
     YKLEDIPADL MLEAKQKGYA DRQIAHLVHR LESEVAAQRH ELGIKRAYKC VDTCAAEFEA
     QTPYYYSTFN VKQENPDNES EVSDKKKILV IGSGPNRIGQ GIEFDYSCVH GVLAAKECGY
     ETIMINCNPE TVSTDPDISD KLYFEPVFWE HVYDIIQHEK PEGVIVQLGG QTALKMAEKL
     TKYGIKIIGT SWEALDLAED RGRFSEKLVE LGIPYPKFTT VRTSDKAVEV SKELGFPLLV
     RPSYVLGGQS MKIVINEDEL EQHVVRILSE IPDNNILLDH FLEGAVEAEA DAICDGEEAY
     IIGIMEHIEP AGIHSGDSYA VLPAFDLSEN VLAQIEDYTK RIAVALDTKG LINIQFAIKD
     EIVYVIEANP RASRTVPFIC KAYQEPYVNY ATQVMLGEKK VKDFNFQPVK KGYAIKIPVF
     SFHKFPNVNK ELGPEMKSTG EGIYFIDNLK DEYFLKVYKE RNMYMSR
//