ID   A0A1M5PXD4_9FIRM        Unreviewed;       356 AA.
AC   A0A1M5PXD4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
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=SAMN02745221_01602 {ECO:0000313|EMBL:SHH06535.1};
OS   Thermosyntropha lipolytica DSM 11003.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Syntrophomonadaceae;
OC   Thermosyntropha.
OX   NCBI_TaxID=1123382 {ECO:0000313|EMBL:SHH06535.1, ECO:0000313|Proteomes:UP000242329};
RN   [1] {ECO:0000313|EMBL:SHH06535.1, ECO:0000313|Proteomes:UP000242329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11003 {ECO:0000313|EMBL:SHH06535.1,
RC   ECO:0000313|Proteomes:UP000242329};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01209};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01209}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|HAMAP-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
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01209}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000256|HAMAP-
CC       Rule:MF_01209}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01209,
CC       ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR   EMBL; FQWY01000027; SHH06535.1; -; Genomic_DNA.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000242329; 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; -; 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   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SMART; SM01097; CPSase_sm_chain; 1.
DR   SUPFAM; SSF52021; SSF52021; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 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|HAMAP-Rule:MF_01209};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000242329};
KW   Glutamine amidotransferase {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01209};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01209}.
FT   DOMAIN      175    356       Glutamine amidotransferase type-1.
FT                                {ECO:0000259|PROSITE:PS51273}.
FT   REGION        1    174       CPSase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01209}.
FT   COILED      143    163       {ECO:0000256|SAM:Coils}.
FT   ACT_SITE    337    337       {ECO:0000256|HAMAP-Rule:MF_01209}.
SQ   SEQUENCE   356 AA;  39173 MW;  CB9A6F9A2988A205 CRC64;
     MMKKGYLVLE NGRVFTGKLL NDCLLAGGEV VFTTAMISYQ DIITDPSYYG QIVVMTYPLV
     GNVGLNEKSY ASRGAMVKGL VLREATDFPS HYEMETDLIS FLNKSEVAVL TEVDTRALTR
     VLRNEGIMGG VITADISHKD WLVEKARKEA EELKGDLVKY VSRRNIMKFG AGKKRVVLLD
     LGTKRGVIDS FIRRGCEVVA VPADTGWDEI LNLNPDGVFI SDGPGDPSAV PYAINTCREV
     LGKKPVFGIG LGHQILALAL GAGINKLPFG HRGGNQPVKD MKNGRVYITT QNHGYCIDEK
     TIDGTGLQVT MRNLNDNTIE AVEHEKMPAF SVQFDPEGYP GYSETGFLFE KFISMF
//