OTC_PYRAB
ID OTC_PYRAB Reviewed; 317 AA.
AC O93656; G8ZHC8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01109};
DE Short=OTCase {ECO:0000255|HAMAP-Rule:MF_01109};
DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN Name=argF {ECO:0000255|HAMAP-Rule:MF_01109}; OrderedLocusNames=PYRAB13230;
GN ORFNames=PAB1502;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RA Cunin R., Seumois G., Purcarea C., Van Vliet F., Legrain C.;
RT "Ornithine carbamoyltransferase from Pyrococcus abyssi.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC produce L-citrulline. {ECO:0000250}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01109};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_01109}.
CC -!- SUBUNIT: Homododecamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01109}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000255|HAMAP-Rule:MF_01109}.
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DR EMBL; AF083209; AAD09004.1; -; Genomic_DNA.
DR EMBL; AJ248287; CAB50228.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE70765.1; -; Genomic_DNA.
DR PIR; G75041; G75041.
DR RefSeq; WP_010868438.1; NC_000868.1.
DR AlphaFoldDB; O93656; -.
DR SMR; O93656; -.
DR STRING; 272844.PAB1502; -.
DR EnsemblBacteria; CAB50228; CAB50228; PAB1502.
DR GeneID; 1496711; -.
DR KEGG; pab:PAB1502; -.
DR PATRIC; fig|272844.11.peg.1408; -.
DR eggNOG; arCOG00912; Archaea.
DR HOGENOM; CLU_043846_3_2_2; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 43727at2157; -.
DR PhylomeDB; O93656; -.
DR BRENDA; 2.1.3.3; 5242.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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 GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1370; -; 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 Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00102; OTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
DR TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..317
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000113071"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 166
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 230
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 234..235
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 270..271
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 298
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT CONFLICT 63
FT /note="S -> R (in Ref. 1; AAD09004)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="A -> G (in Ref. 1; AAD09004)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="V -> I (in Ref. 1; AAD09004)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..202
FT /note="EQ -> DE (in Ref. 1; AAD09004)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="D -> S (in Ref. 1; AAD09004)"
FT /evidence="ECO:0000305"
FT CONFLICT 313..316
FT /note="VKTG -> RKDGLLT (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35358 MW; F4686B091F76494F CRC64;
MVVSLKGRDL LCLQDYTPEE IWTILETAKM LKIWQKIGKP HRLLEGKTLA MIFQKPSTRT
RVSFEVAMAH LGGHALYLNA QDLQLRRGET IADTARVLSR YVDAIMARVY DHKDVEDLAK
YASVPVINGL SDFSHPCQAL ADYMTIWEKK GTIKGVKVVY VGDGNNVAHS LMIAGTKLGA
DVVVATPEGY EPDEKVIKWA EQNAAESGGS FELLHDPVKA VKDADVIYTD VWASMGQEAE
AEERRKIFRP FQVNKDLVKH AKPDYMFMHC LPAHRGEEVT DDVIDSPNSV VWDEAENRLH
AQKAVLALLL GGVKTGF
