ID   CARA_BACSU              Reviewed;         364 AA.
AC   P25993;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Carbamoyl-phosphate synthase pyrimidine-specific small chain;
DE            EC=6.3.5.5;
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain;
GN   Name=pyrAA; OrderedLocusNames=BSU15510;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1709162; DOI=10.1016/s0021-9258(18)31559-x;
RA   Quinn C.L., Stephenson B.T., Switzer R.L.;
RT   "Functional organization and nucleotide sequence of the Bacillus subtilis
RT   pyrimidine biosynthetic operon.";
RL   J. Biol. Chem. 266:9113-9127(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   INTERACTION WITH BRXC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=168 / CU1065 {ECO:0000303|PubMed:33722570};
RX   PubMed=33722570; DOI=10.1016/j.redox.2021.101935;
RA   Gaballa A., Su T.T., Helmann J.D.;
RT   "The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr
RT   (YpdA) disulfide reductase reduce S-bacillithiolated proteins.";
RL   Redox Biol. 42:101935-101935(2021).
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
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 (By
CC       similarity). Interacts with BrxC (PubMed:33722570).
CC       {ECO:0000250|UniProtKB:P0A6F1, ECO:0000269|PubMed:33722570}.
CC   -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}.
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DR   EMBL; M59757; AAA21269.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13425.1; -; Genomic_DNA.
DR   PIR; E39845; E39845.
DR   RefSeq; NP_389434.1; NC_000964.3.
DR   RefSeq; WP_003232115.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P25993; -.
DR   SMR; P25993; -.
DR   STRING; 224308.BSU15510; -.
DR   PaxDb; P25993; -.
DR   PRIDE; P25993; -.
DR   EnsemblBacteria; CAB13425; CAB13425; BSU_15510.
DR   GeneID; 937368; -.
DR   KEGG; bsu:BSU15510; -.
DR   PATRIC; fig|224308.179.peg.1690; -.
DR   eggNOG; COG0505; Bacteria.
DR   InParanoid; P25993; -.
DR   OMA; CFNTGMT; -.
DR   PhylomeDB; P25993; -.
DR   BioCyc; BSUB:BSU15510-MON; -.
DR   BioCyc; MetaCyc:BSU15510-MON; -.
DR   SABIO-RK; P25993; -.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..364
FT                   /note="Carbamoyl-phosphate synthase pyrimidine-specific
FT                   small chain"
FT                   /id="PRO_0000112255"
FT   DOMAIN          171..356
FT                   /note="Glutamine amidotransferase type-1"
FT   REGION          1..167
FT                   /note="CPSase"
FT   ACT_SITE        246
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        329
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        331
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   364 AA;  40119 MW;  676304F876709FC0 CRC64;
     MKRRLVLENG AVFEGEAFGS LEHNMGEVVF NTGMTGYQEI LSDPSYCGQI VTLTYPLIGN
     YGINRDDFES ITPFVKGLII KELCELPSNW RSAYTLDEYL KMKNIPGLQG IDTRKLTRMI
     RTAGALKGTF ASSDEDIEAV LKRLNETELP RNQVSQVSAK TAYPSPGRGK RIVLVDFGMK
     HGILRELNKR KCDVIVVPYN ITAEEVLQLK PDGIMLSNGP GDPKDVPEAI EMIKGVLGKV
     PLFGICLGHQ LFALACGANT EKMKFGHRGS NHPVKELATG KVALTSQNHG YTVSSISKTE
     LEVTHIAIND DTIEGLKHKT LPAFTVQYHP EASPGPEDAN HLFDRFIEMI ETTEKEGEAV
     CQNA