ID D6BV77_POPCN Unreviewed; 400 AA.
AC D6BV77;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=carbamoyl-phosphate synthase (glutamine-hydrolyzing) {ECO:0000256|ARBA:ARBA00012738};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE Flags: Fragment;
GN Name=CPS {ECO:0000313|EMBL:ADB92668.1};
OS Populus canescens (Grey poplar) (Populus tremula x Populus alba).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=80863 {ECO:0000313|EMBL:ADB92668.1};
RN [1] {ECO:0000313|EMBL:ADB92668.1}
RP NUCLEOTIDE SEQUENCE.
RA Wildhagen H., Ehlting B., Rennenberg H.;
RT "Seasonal nitrogen cycling in grey poplar (Populus tremula x Populus
RT alba).";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000256|ARBA:ARBA00043737};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SUBUNIT: Heterodimer composed of 2 chains; the small (or glutamine)
CC chain promotes the hydrolysis of glutamine to ammonia, which is used by
CC the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000256|ARBA:ARBA00044031}.
CC -!- SIMILARITY: Belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00007800}.
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DR EMBL; FJ943650; ADB92668.1; -; mRNA.
DR AlphaFoldDB; D6BV77; -.
DR MEROPS; C26.A04; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01744; GATase1_CPSase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.50.30.20; Carbamoyl-phosphate synthase small subunit, N-terminal domain; 1.
DR HAMAP; MF_01209; CPSase_S_chain; 1.
DR InterPro; IPR006274; CarbamoylP_synth_ssu.
DR InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR InterPro; IPR036480; CarbP_synth_ssu_N_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035686; CPSase_GATase1.
DR InterPro; IPR017926; GATASE.
DR NCBIfam; TIGR01368; CPSaseIIsmall; 1.
DR PANTHER; PTHR11405:SF4; CARBAMOYL-PHOSPHATE SYNTHASE ARGININE-SPECIFIC SMALL CHAIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF00988; CPSase_sm_chain; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SMART; SM01097; CPSase_sm_chain; 1.
DR SUPFAM; SSF52021; Carbamoyl phosphate synthetase, small subunit N-terminal domain; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADB92668.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 47..177
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 392
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADB92668.1"
FT NON_TER 400
FT /evidence="ECO:0000313|EMBL:ADB92668.1"
SQ SEQUENCE 400 AA; 43798 MW; 442CC9CBB8490B66 CRC64;
IAPTTQNFLK PKPKVKSLRV FSLKCVSSLS SSDGAATGVV ERPWKTSDAR LVLEDGSVWR
AKSFGARGTQ VGEVVFNTSL TGYQEILTDP SYAGQFVLMT NPHIGNTGVN FDDEESRQCF
LAGLVIRSLS ISTSNWRCTK ELGDYLLERN IMGIYDVDTR AITRRLRQDG SLVGVLTTEE
SKTDEELLKM SRSWDIEGID LISGVSCTAP YEWVGKTDLE WDFNREGRGE IYHVVAYDFG
IKHNILRRLA SYGCKITVVP SKWPASETLK MKPDGVLFSN GPGDPSAVPY AVETVKELLG
KVPVFGICMG HQLLGQALGG KTFKMKFGHH GGNHPVRNLL ANRVEISAQN HNYAVDPASL
PEGVEVTHIN LNDGSCAGLA FPALNVMSLQ YHPEASPGPH
//
