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Database: UniProt
Entry: H1Q216_9BACT
LinkDB: H1Q216_9BACT
Original site: H1Q216_9BACT 
ID   H1Q216_9BACT            Unreviewed;       359 AA.
AC   H1Q216;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=HMPREF9140_00989 {ECO:0000313|EMBL:EHO71249.1};
OS   Prevotella micans F0438.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=883158 {ECO:0000313|EMBL:EHO71249.1, ECO:0000313|Proteomes:UP000016023};
RN   [1] {ECO:0000313|EMBL:EHO71249.1, ECO:0000313|Proteomes:UP000016023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0438 {ECO:0000313|EMBL:EHO71249.1,
RC   ECO:0000313|Proteomes:UP000016023};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA   Blanton J.M., Wade W.G., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA   McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella micans F0438.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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: 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:EHO71249.1}.
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DR   EMBL; AGWK01000028; EHO71249.1; -; Genomic_DNA.
DR   RefSeq; WP_006952197.1; NZ_JH594522.1.
DR   AlphaFoldDB; H1Q216; -.
DR   STRING; 883158.HMPREF9140_00989; -.
DR   PATRIC; fig|883158.3.peg.998; -.
DR   eggNOG; COG0505; Bacteria.
DR   HOGENOM; CLU_035901_1_1_10; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000016023; 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-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   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|HAMAP-Rule:MF_01209,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016023}.
FT   DOMAIN          2..141
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   REGION          1..177
FT                   /note="CPSase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        336
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        338
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   359 AA;  39836 MW;  E1844715E6740286 CRC64;
     MRNVTLILND GTRFHGKSFG YEKPVAGEVV FNTAMMGYPE SLTDPSYAGQ MIVTTFPLVG
     NYGVPPLTIG SDGIPLFMES NRIHASALIV AHYSEHHSHW NAAMSLAQWL KNEQVPGITD
     IDTRELTKVL REHGVMMGKI ILDDEPNNIP EADYEGVNFV DSVSTKEIIR YNEGAGKKVV
     LVDCGVKANI IRSLVKRGVE VIRVPWNYDY ISLDFDGLFL ANGPGDPDTC QVAVDIIRKQ
     MNQSIKPICG ICMGNQLLAK AAGASIYKLK YGHRGHNQPV RMVGTERCYV TSQNHGYAVD
     AASLGADWEE LFVNMNDGSN EGIRHKTNPW FSSQFHPEAC SGPVDTYFMF DKFVEILQK
//
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