ID   G6E6R4_9SPHN            Unreviewed;       388 AA.
AC   G6E6R4;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAY-2015, entry version 22.
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=NSU_0035 {ECO:0000313|EMBL:EHJ62960.1};
OS   Novosphingobium pentaromativorans US6-1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1088721 {ECO:0000313|EMBL:EHJ62960.1, ECO:0000313|Proteomes:UP000004030};
RN   [1] {ECO:0000313|EMBL:EHJ62960.1, ECO:0000313|Proteomes:UP000004030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=US6-1 {ECO:0000313|EMBL:EHJ62960.1};
RX   PubMed=22275104; DOI=10.1128/JB.06476-11;
RA   Luo Y.R., Kang S.G., Kim S.J., Kim M.R., Li N., Lee J.H., Kwon K.K.;
RT   "Genome sequence of benzo(a)pyrene-degrading bacterium Novosphingobium
RT   pentaromativorans US6-1.";
RL   J. Bacteriol. 194:907-907(2012).
CC   -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2
CC       ADP + phosphate + L-glutamate + carbamoyl phosphate.
CC       {ECO:0000256|HAMAP-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   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC       {ECO:0000256|HAMAP-Rule:MF_01209}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EHJ62960.1}.
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DR   EMBL; AGFM01000002; EHJ62960.1; -; Genomic_DNA.
DR   RefSeq; WP_007010952.1; NZ_AGFM01000002.1.
DR   EnsemblBacteria; AIT78437; AIT78437; JI59_00650.
DR   EnsemblBacteria; EHJ62960; EHJ62960; NSU_0035.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000004030; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070409; P:carbamoyl phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006543; P:glutamine catabolic process; IEA:InterPro.
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; IPR029062; Class_I_gatase-like.
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   Complete proteome {ECO:0000313|Proteomes:UP000004030};
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   REGION        1    201       CPSase. {ECO:0000256|HAMAP-Rule:
FT                                MF_01209}.
FT   ACT_SITE    282    282       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01209}.
FT   ACT_SITE    366    366       {ECO:0000256|HAMAP-Rule:MF_01209}.
FT   ACT_SITE    368    368       {ECO:0000256|HAMAP-Rule:MF_01209}.
SQ   SEQUENCE   388 AA;  41229 MW;  00E10755DFD1BF2C CRC64;
     MADAAFSLAP KPEGATGVLV LSDGHVIWGR GFGAVGNAVG EVCFNTSMTG YQEVMTDPSY
     AGQIVTFTFP HIGNVGVNDE DLESRVDSAV GCVVREDVTP SSNFRAEGEF GDWLAAKGKI
     GLAGVDTRAL TRRIRLSGAP NAVIAHDPKG EFDIPALIKK AQEWPGLEGM DLAKIVSREH
     QEGWEGSTWT LGQGYGRSPR DERPHVVAMD FGAKDNIFRN LVKAGARVTV VPAEATLDQV
     LELKPQGVFL SNGPGDPAAT GKYAVPVIQG LLERDVPIFG ICLGHQMLAL AAGASTSKMH
     QGHRGANHPV KRLADDVVEI TSMNHGFAVD NATLPDTIEE THVSLFDGSN CGIAIKGKKA
     FGVQYHPEAS PGPQDSFYLF EKFVGALA
//