位置:首页 > 蛋白库 > OTC_PYRAB
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024