ID F2SPM6_TRIRC Unreviewed; 474 AA.
AC F2SPM6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Carbamoyl-phosphate synthase arginine-specific small chain {ECO:0000256|ARBA:ARBA00040852};
DE EC=6.3.5.5 {ECO:0000256|ARBA:ARBA00012738};
DE AltName: Full=Arginine-specific carbamoyl-phosphate synthetase, glutamine chain {ECO:0000256|ARBA:ARBA00042128};
GN ORFNames=TERG_04024 {ECO:0000313|EMBL:EGD87778.1};
OS Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD87778.1, ECO:0000313|Proteomes:UP000008864};
RN [1] {ECO:0000313|Proteomes:UP000008864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
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|ARBA:ARBA00011275}.
CC -!- SIMILARITY: Belongs to the CarA family.
CC {ECO:0000256|ARBA:ARBA00007800}.
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DR EMBL; GG700651; EGD87778.1; -; Genomic_DNA.
DR RefSeq; XP_003234973.1; XM_003234925.1.
DR AlphaFoldDB; F2SPM6; -.
DR STRING; 559305.F2SPM6; -.
DR GeneID; 10376277; -.
DR VEuPathDB; FungiDB:TERG_04024; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_035901_1_0_1; -.
DR InParanoid; F2SPM6; -.
DR OMA; CFNTGMT; -.
DR OrthoDB; 2783936at2759; -.
DR Proteomes; UP000008864; Unassembled WGS sequence.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008864}.
FT DOMAIN 56..195
FT /note="Carbamoyl-phosphate synthase small subunit N-
FT terminal"
FT /evidence="ECO:0000259|SMART:SM01097"
FT ACT_SITE 312
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 396
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 474 AA; 51453 MW; C03F5E8007DCFD1E CRC64;
MFAARAFRSL PFKVHAAHGL PQRFGGQLGG QTRMMAFVVN GGPMSAKAPS APSAIERATL
TIRNGPIFHG KSFGAKTNIS GEAVFTTSLV GYPESLSDPS YRGQILVFTQ PLIGNYGIPS
SERDEHGLLK YFESPSLQAV GVVVADAALK YSHWTAVESL SEWCIREGVP AISGVDTRQI
VTYLREQGSS LARITVGEEY DADQDEAFID PEQINLVRKV STKSPFHVSA ANSTSHVAVI
DCGVKENILR SLVSRGASVT VFPYDYPVYK VAHHFDGVFI SNGPGDPTHC SQTVHTLSKL
MQTSQIPIMG ICLGHQLLAL AVGARTIKLK YGNRAHNIPA LDLTTGRCHI TSQNHGYAVD
ASTLPSDWKP YFVNLNDNSN EGMIHKTRPI FSTQFHPEAK GGPLDSSYLF DIYLDSVQKY
KANQAIHQPG RDNRPSPLLA DLLGNERVGV SIDRESYMTS SPEEPAQNLA AATA
//