ID G6F7S2_LACDE Unreviewed; 361 AA.
AC G6F7S2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000256|HAMAP-Rule:MF_01209};
DE EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01209};
DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000256|HAMAP-Rule:MF_01209};
GN Name=carA {ECO:0000256|HAMAP-Rule:MF_01209};
GN ORFNames=LDBUL1519_01458 {ECO:0000313|EMBL:EHE88170.1};
OS Lactobacillus delbrueckii subsp. bulgaricus CNCM I-1519.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1042400 {ECO:0000313|EMBL:EHE88170.1, ECO:0000313|Proteomes:UP000003923};
RN [1] {ECO:0000313|EMBL:EHE88170.1, ECO:0000313|Proteomes:UP000003923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1519 {ECO:0000313|EMBL:EHE88170.1,
RC ECO:0000313|Proteomes:UP000003923};
RX PubMed=22030749;
RA McNulty N.P., Yatsunenko T., Hsiao A., Faith J.J., Muegge B.D.,
RA Goodman A.L., Henrissat B., Oozeer R., Cools-Portier S., Gobert G.,
RA Chervaux C., Knights D., Lozupone C.A., Knight R., Duncan A.E., Bain J.R.,
RA Muehlbauer M.J., Newgard C.B., Heath A.C., Gordon J.I.;
RT "The impact of a consortium of fermented milk strains on the gut microbiome
RT of gnotobiotic mice and monozygotic twins.";
RL Sci. Transl. Med. 3:106RA106-106RA106(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:456216; EC=6.3.5.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001777, ECO:0000256|HAMAP-
CC Rule:MF_01209};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01209}.
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000256|HAMAP-
CC Rule:MF_01209}.
CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC promotes the hydrolysis of glutamine to ammonia, which is used by the
CC large (or ammonia) chain to synthesize carbamoyl phosphate.
CC {ECO:0000256|HAMAP-Rule:MF_01209}.
CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|ARBA:ARBA00007800,
CC ECO:0000256|HAMAP-Rule:MF_01209}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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:EHE88170.1}.
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DR EMBL; AGHW01000041; EHE88170.1; -; Genomic_DNA.
DR RefSeq; WP_003623965.1; NZ_AGHW01000041.1.
DR AlphaFoldDB; G6F7S2; -.
DR PATRIC; fig|1042400.3.peg.1450; -.
DR UniPathway; UPA00068; UER00171.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000003923; 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-UniRule.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01209};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_01209};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01209};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01209}; Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}.
FT DOMAIN 1..130
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT REGION 1..169
FT /note="CPSase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT ACT_SITE 245
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT ACT_SITE 330
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT ACT_SITE 332
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
SQ SEQUENCE 361 AA; 40359 MW; 6932B8D33C5DF937 CRC64;
MRYLILEDGS IYAGEGFGSD RETTGEVVFT TGMTGYQEAI TDQSYADQIL VFTNPLIGNY
GITLADYESL QPQIKGVICH QIARHPDNWR MQTTLPEFLK QLHIPGIQGI DTRELVKKLR
VHGTLRGKIA NSKENAEKIV QELKHKNVTQ GVISRVSTKS AYPVPGSKRN IVVIDFGIKH
SILRELAERD CNCIVLPYTA TAEEVLNLHP DGVLLSNGPG DPEEMIEATK MVQEVEKHVP
LFGICMGHQV FALANGAKTY KMKFGHRGFN HPVREIATGH IGFTSQNHGY AVDAKSIDKD
NLMITHEEVN DGTVEGLRHK KYPAFSVQFH PDATPGPHDE DSLFDDFMSM IDQRKEEERH
A
//