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OTC_NEIPE
ID   OTC_NEIPE               Reviewed;         232 AA.
AC   O86404; O86405;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Ornithine carbamoyltransferase;
DE            Short=OTCase;
DE            EC=2.1.3.3;
DE   Flags: Fragment;
GN   Name=argF;
OS   Neisseria perflava.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=33053;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10555 / DSM 18009 / CIP 73.11 / CCUG 17915 / LMG 5284 / NRL
RC   30015 / NRRL B-1790, and LCDC 85402;
RX   PubMed=10368955; DOI=10.1093/oxfordjournals.molbev.a026162;
RA   Smith N.H., Holmes E.C., Donovan G.M., Carpenter G.A., Spratt B.G.;
RT   "Networks and groups within the genus Neisseria: analysis of argF, recA,
RT   rho, and 16S rRNA sequences from human Neisseria species.";
RL   Mol. Biol. Evol. 16:773-783(1999).
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;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000305}.
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DR   EMBL; AJ223883; CAA11614.1; -; Genomic_DNA.
DR   EMBL; AJ223897; CAA11628.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86404; -.
DR   SMR; O86404; -.
DR   UniPathway; UPA00068; UER00112.
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-EC.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1370; -; 2.
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   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm; Transferase.
FT   CHAIN           <1..>232
FT                   /note="Ornithine carbamoyltransferase"
FT                   /id="PRO_0000112968"
FT   BINDING         15
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..69
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         99
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..207
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   BINDING         232
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000250"
FT   SITE            79
FT                   /note="Important for structural integrity"
FT                   /evidence="ECO:0000250"
FT   VARIANT         6
FT                   /note="A -> V (in strain: CCUG 17915L)"
FT   VARIANT         33..35
FT                   /note="YDA -> FDG (in strain: CCUG 17915L)"
FT   VARIANT         44..46
FT                   /note="EII -> DVV (in strain: CCUG 17915L)"
FT   VARIANT         82
FT                   /note="S -> N (in strain: CCUG 17915L)"
FT   VARIANT         88
FT                   /note="T -> I (in strain: CCUG 17915L)"
FT   VARIANT         101
FT                   /note="G -> A (in strain: CCUG 17915L)"
FT   VARIANT         106..108
FT                   /note="ILG -> VLA (in strain: CCUG 17915L)"
FT   VARIANT         121
FT                   /note="E -> K (in strain: CCUG 17915L)"
FT   VARIANT         128..134
FT                   /note="GIIAAAH -> NIIETVQ (in strain: CCUG 17915L)"
FT   VARIANT         142..145
FT                   /note="AKIT -> GRIL (in strain: CCUG 17915L)"
FT   VARIANT         150..151
FT                   /note="AH -> VK (in strain: CCUG 17915L)"
FT   VARIANT         155
FT                   /note="N -> K (in strain: CCUG 17915L)"
FT   VARIANT         158
FT                   /note="G -> D (in strain: CCUG 17915L)"
FT   VARIANT         174
FT                   /note="V -> A (in strain: CCUG 17915L)"
FT   VARIANT         195..196
FT                   /note="SG -> AE (in strain: CCUG 17915L)"
FT   NON_TER         1
FT   NON_TER         232
SQ   SEQUENCE   232 AA;  25480 MW;  E750AF7DD8FA3816 CRC64;
     DQGAGATYLE PSASQIGHKE SIKDTARVLG RMYDAIEYRG FGQEIIEELA KYAGVPVFNG
     LTNEFHPTQM LADALTMREH SSKPLNQTAF AYVGDARYNM GNSLLILGAK LGMDVRIGAP
     ESLWPSEGII AAAHAVAKET GAKITLTENA HEAVNGVGFI HTDVWVSMGE PKEVWQERID
     LLKDYRVTPE LMAASGNPQV KFMHCLPAFH NRETKVGEWI YETFGLNGVE VT
 
 
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