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Database: UniProt
Entry: A0A1L8CKQ3_9PROT
LinkDB: A0A1L8CKQ3_9PROT
Original site: A0A1L8CKQ3_9PROT 
ID   A0A1L8CKQ3_9PROT        Unreviewed;       371 AA.
AC   A0A1L8CKQ3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Carbamoyl-phosphate synthase small chain {ECO:0000256|ARBA:ARBA00019036, ECO:0000256|HAMAP-Rule:MF_01209};
DE            EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738, ECO:0000256|HAMAP-Rule:MF_01209};
DE   AltName: Full=Carbamoyl-phosphate synthetase glutamine chain {ECO:0000256|ARBA:ARBA00030197, ECO:0000256|HAMAP-Rule:MF_01209};
GN   Name=carA {ECO:0000256|HAMAP-Rule:MF_01209};
GN   ORFNames=MMIC_P0399 {ECO:0000313|EMBL:GAV19465.1};
OS   Mariprofundus micogutta.
OC   Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC   Mariprofundaceae; Mariprofundus.
OX   NCBI_TaxID=1921010 {ECO:0000313|EMBL:GAV19465.1, ECO:0000313|Proteomes:UP000231632};
RN   [1] {ECO:0000313|EMBL:GAV19465.1, ECO:0000313|Proteomes:UP000231632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ET2 {ECO:0000313|EMBL:GAV19465.1,
RC   ECO:0000313|Proteomes:UP000231632};
RX   PubMed=27766355; DOI=10.1007/s00203-016-1307-4;
RA   Makita H., Tanaka E., Mitsunobu S., Miyazaki M., Nunoura T., Uematsu K.,
RA   Takaki Y., Nishi S., Shimamura S., Takai K.;
RT   "Mariprofundus micogutta sp. nov., a novel iron-oxidizing
RT   zetaproteobacterium isolated from a deep-sea hydrothermal field at the
RT   Bayonnaise knoll of the Izu-Ogasawara arc, and a description of
RT   Mariprofundales ord. nov. and Zetaproteobacteria classis nov.";
RL   Arch. Microbiol. 199:335-346(2017).
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|ARBA:ARBA00005077,
CC       ECO:0000256|HAMAP-Rule:MF_01209}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004812, 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 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:GAV19465.1}.
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DR   EMBL; BDFD01000002; GAV19465.1; -; Genomic_DNA.
DR   RefSeq; WP_072658646.1; NZ_BDFD01000002.1.
DR   AlphaFoldDB; A0A1L8CKQ3; -.
DR   STRING; 1921010.MMIC_P0399; -.
DR   OrthoDB; 5288626at2; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000231632; 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}.
FT   DOMAIN          2..132
FT                   /note="Carbamoyl-phosphate synthase small subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|SMART:SM01097"
FT   REGION          1..187
FT                   /note="CPSase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209"
FT   ACT_SITE        264
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        348
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01209,
FT                   ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   371 AA;  39922 MW;  C7EC81AFDA432DCA CRC64;
     MAKAILALAD GRIFRGEALG AIGNTVGEVC FNTSLTGYQE ILTDPSYTDQ IITFTYPHIG
     NVGVNETDME SDAISVRGCI VRAPARITSN YRAEKDLAAW LSDNSVVGIA DIDTRALVRH
     LRDHGAQNGV IASDGMSEAD AVAMAKAWDG LEGRDLVGQV SCKQKGEWQQ GTYNLDAASF
     NSPASDKHVV AFDFGCKRNI FRKLADRGLN VTVVPAQTPA TAVLALNPDG IFLSNGPGDP
     AAVAYAVETI RELLDSNVPI FGICMGHQLL SQALGLSTFK LKFGHRGGNH PVKDLTTGKI
     EITSQNHGFA VADDNIPENV EITHRSLFDE TVEGLCVKEK AIFSVQYHPE ASPGPQDADY
     LFDRFAEIIK S
//
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