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Database: UniProt
Entry: F2L0J5_THEU7
LinkDB: F2L0J5_THEU7
Original site: F2L0J5_THEU7 
ID   F2L0J5_THEU7            Unreviewed;       307 AA.
AC   F2L0J5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=ornithine carbamoyltransferase {ECO:0000256|ARBA:ARBA00013007};
DE            EC=2.1.3.3 {ECO:0000256|ARBA:ARBA00013007};
GN   OrderedLocusNames=TUZN_1198 {ECO:0000313|EMBL:AEA12677.1};
OS   Thermoproteus uzoniensis (strain 768-20).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=999630 {ECO:0000313|EMBL:AEA12677.1, ECO:0000313|Proteomes:UP000008138};
RN   [1] {ECO:0000313|EMBL:AEA12677.1, ECO:0000313|Proteomes:UP000008138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=768-20 {ECO:0000313|EMBL:AEA12677.1,
RC   ECO:0000313|Proteomes:UP000008138};
RX   PubMed=21478349; DOI=10.1128/JB.00409-11;
RA   Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of the thermoacidophilic crenarchaeon
RT   Thermoproteus uzoniensis 768-20.";
RL   J. Bacteriol. 193:3156-3157(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=768-20;
RA   Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of the thermoacidophilic crenarchaeon
RT   Thermoproteus uzoniensis 768-20.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC         phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:58228; EC=2.1.3.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001065, ECO:0000256|HAMAP-
CC         Rule:MF_01109};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000256|ARBA:ARBA00007805,
CC       ECO:0000256|HAMAP-Rule:MF_01109}.
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DR   EMBL; CP002590; AEA12677.1; -; Genomic_DNA.
DR   RefSeq; WP_013680013.1; NC_015315.1.
DR   AlphaFoldDB; F2L0J5; -.
DR   STRING; 999630.TUZN_1198; -.
DR   GeneID; 10360726; -.
DR   KEGG; tuz:TUZN_1198; -.
DR   eggNOG; arCOG00912; Archaea.
DR   HOGENOM; CLU_043846_3_2_2; -.
DR   OMA; DGNNVCN; -.
DR   OrthoDB; 4696at2157; -.
DR   Proteomes; UP000008138; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   HAMAP; MF_01109; OTCase; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002292; Orn/put_carbamltrans.
DR   InterPro; IPR024904; OTCase_ArgI.
DR   NCBIfam; TIGR00658; orni_carb_tr; 1.
DR   PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01109}.
FT   DOMAIN          5..146
FT                   /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02729"
FT   DOMAIN          152..304
FT                   /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF00185"
FT   BINDING         55..58
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         82
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         106
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         133..136
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         165
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         226
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         230..231
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         266..267
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
FT   BINDING         294
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   307 AA;  33987 MW;  4BE40E3EFBB7C912 CRC64;
     MFRGRDVLTL MEFRPDEVVA LLEMAKGFKA RYHAGEVYTP IHLGKTAVLI FEKPSTRTRV
     STSAAAYQLG MNVIVANPQE LQLGRGETVP DTARTLSRYA HVIAARVFKH ETLEELAQYA
     DVPVLNLLSD KFHPLQSLAD ALTLWEKKGR LNGLKVAFVG DVGNNVAASL AVIGSKLGWE
     VRLVGPRQLW RNDLSRLAED AGLTGARVYQ TDSLEELKGV DAVYTDVWVS MGFEKEAEER
     ERLLRPYQVN ASVMELAGPQ ALFMHCLPAH RGMEVTDDVI DGPRSVVWDQ AENRLHTAKA
     VLAAVTP
//
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