ID A0A1Q7F6F4_9CHLR Unreviewed; 935 AA.
AC A0A1Q7F6F4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carbamoyl phosphate synthase large subunit {ECO:0000313|EMBL:OLC22284.1};
DE Flags: Fragment;
GN ORFNames=AUH36_02395 {ECO:0000313|EMBL:OLC22284.1};
OS Chloroflexi bacterium 13_1_40CM_55_7.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1805079 {ECO:0000313|EMBL:OLC22284.1, ECO:0000313|Proteomes:UP000187540};
RN [1] {ECO:0000313|EMBL:OLC22284.1, ECO:0000313|Proteomes:UP000187540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
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:OLC22284.1}.
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DR EMBL; MNET01000046; OLC22284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7F6F4; -.
DR Proteomes; UP000187540; 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; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 139..334
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 685..888
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT NON_TER 935
FT /evidence="ECO:0000313|EMBL:OLC22284.1"
SQ SEQUENCE 935 AA; 102912 MW; A72AC0E1ACC7C78D CRC64;
MPRRTDISKI LIIGSGPIII GQSAEFDYSG TQACKALKAE GFEVVLANSN PATIMTDPEI
ADRTYIEPLT RDYLEEIIRV ERELSPGKGF AILPTVGGQT ALNLAVELSD GGILDKYNVQ
LIGANIAAIK KAEDRLYFKD AMQKIGLDVP KSALVNNLKD GLEFAGKIGF PVIVRPSFTL
GGSGGGIAYN REELVEVLAR GLDFSPVHEA LIEESVLGWK EYELEVMRDM RDNVIIICSI
ENFDPMGVHT GDSITVAPAQ TLTDREYQAM RDAAIAVIRE IGVETGGSNI QFGVNPTSGR
IVVIEMNPRV SRSSALASKA TGFPIAKIAA KLAVGYTLDE IPNDITRKTP ACFEPTLDYV
VVKIPKWQFE KFPGADESLG PQMKSVGEVM AIGRTFKEAL LKGVRALDTG KKVGSEKIEP
KILTQRLVTP HPERLSYVRY ALRQGHTVKQ LAKMTSIDPW FLYQLKEINE MQLELEKHPM
ESIPTEVLRE AKRMGFSDGR LASVWRLSGK SGQEKVRHLR KKRGIMPVYK RVDTCAAEFE
SYTPYLYSTY EDEDEAAPTK KKKVIILGSG PNRIGQGIEF DYCCCHAAFA LRDDGYETIM
INCNPETVST DYDTSDRLYF EPLTLEDVFA IYEHEAASGV SVGLIVQFGG QTPLNLPLPL
KAAGVNIIGT SPESIDLAED RKRFGKLLDE LDIPQAPGAM AASVEEAIEG AKRVQYPVLV
RPSYVLGGRA MVIAYDEETV VRYMKEAVEF SHDRPVLIDH FLEDAIEVDV DALSDGEDVV
IGGIMQHIEE AGIHSGDSSC VLPAVDIPEA LLARMREYTF SLARALKVVG LMNIQFAIPR
TNGNSKGNGS EAGKVYVLEV NPRASRTVPY VSKATGVPMA KIAARLMTGR KLREFLPDFI
DRRADLNTGH CYYVKSPVFP WNKFPGIDTV LGPEM
//
