OTC_VIBVU
ID OTC_VIBVU Reviewed; 334 AA.
AC Q8DCF5;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=VV1_1466;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS).
RG Center for structural genomics of infectious diseases (CSGID);
RA Papazisi L., Anderson W.F.;
RT "2.9 angstrom crystal structure of ornithine carbamoyltransferase (argF)
RT from Vibrio vulnificus.";
RL Submitted (NOV-2011) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH CARBAMOYL PHOSPHATE
RP AND SUBSTRATE ANALOGS, AND SUBUNIT.
RA Shabalin I.G., Winsor J., Grimshaw S., Osinski T., Chordia M.D.,
RA Anderson W.F., Minor W.;
RT "Structural studies of ornithine carbamoyltransferase from various
RT pathogens.";
RL Submitted (SEP-2012) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CARBAMOYL PHOSPHATE
RP AND SUBSTRATE ANALOGS, AND SUBUNIT.
RA Shabalin I.G., Winsor J., Grimshaw S., Minor W.;
RT "Crystal structures and kinetic properties of anabolic ornithine
RT carbamoyltransferase from human pathogens Vibrio vulnificus and Bacillus
RT anthracis.";
RL Submitted (FEB-2013) to the PDB data bank.
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:0000255|HAMAP-Rule:MF_01109}.
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: Homotrimer. {ECO:0000305|Ref.3, ECO:0000305|Ref.4}.
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; AE016795; AAO09905.1; -; Genomic_DNA.
DR RefSeq; WP_011079423.1; NC_004459.3.
DR PDB; 3UPD; X-ray; 2.91 A; A=1-334.
DR PDB; 4H31; X-ray; 1.70 A; A/B/C=1-334.
DR PDB; 4JFR; X-ray; 2.17 A; A/B/C=1-334.
DR PDB; 4JHX; X-ray; 1.85 A; A/B/C=1-334.
DR PDB; 4JQO; X-ray; 2.08 A; A/B/C=1-334.
DR PDB; 4KWT; X-ray; 1.86 A; A/B/C=1-334.
DR PDBsum; 3UPD; -.
DR PDBsum; 4H31; -.
DR PDBsum; 4JFR; -.
DR PDBsum; 4JHX; -.
DR PDBsum; 4JQO; -.
DR PDBsum; 4KWT; -.
DR AlphaFoldDB; Q8DCF5; -.
DR SMR; Q8DCF5; -.
DR EnsemblBacteria; AAO09905; AAO09905; VV1_1466.
DR KEGG; vvu:VV1_1466; -.
DR HOGENOM; CLU_043846_3_1_6; -.
DR OMA; VYVKNWS; -.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000002275; Chromosome 1.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Transferase.
FT CHAIN 1..334
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000113056"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:4H31, ECO:0007744|PDB:4JFR,
FT ECO:0007744|PDB:4JHX, ECO:0007744|PDB:4JQO"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:4H31, ECO:0007744|PDB:4JQO"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:4H31, ECO:0007744|PDB:4JFR,
FT ECO:0007744|PDB:4JHX, ECO:0007744|PDB:4JQO"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:4H31, ECO:0007744|PDB:4JFR,
FT ECO:0007744|PDB:4JHX, ECO:0007744|PDB:4JQO"
FT BINDING 169
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:4H31, ECO:0007744|PDB:4JHX,
FT ECO:0007744|PDB:4JQO"
FT BINDING 233
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:4H31, ECO:0007744|PDB:4JHX,
FT ECO:0007744|PDB:4JQO"
FT BINDING 237..238
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:4H31, ECO:0007744|PDB:4JHX,
FT ECO:0007744|PDB:4JQO"
FT BINDING 275..276
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:4H31, ECO:0007744|PDB:4JFR,
FT ECO:0007744|PDB:4JHX, ECO:0007744|PDB:4JQO"
FT BINDING 320
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4,
FT ECO:0007744|PDB:4H31, ECO:0007744|PDB:4JHX,
FT ECO:0007744|PDB:4JQO"
FT HELIX 1..5
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 18..37
FT /evidence="ECO:0007829|PDB:4H31"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4H31"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 136..148
FT /evidence="ECO:0007829|PDB:4H31"
FT TURN 149..152
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 220..224
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:3UPD"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 285..293
FT /evidence="ECO:0007829|PDB:4H31"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 303..306
FT /evidence="ECO:0007829|PDB:4H31"
FT HELIX 313..332
FT /evidence="ECO:0007829|PDB:4H31"
SQ SEQUENCE 334 AA; 36859 MW; 67E1FFDE5B43A064 CRC64;
MAFNLRNRNF LKLLDFSTKE IQFLIDLSAD LKKAKYAGTE QKKLLGKNIA LIFEKASTRT
RCAFEVAAFD QGAQVTYIGP SGSQIGDKES MKDTARVLGR MYDGIQYRGF GQAIVEELGA
FAGVPVWNGL TDEFHPTQIL ADFLTMLEHS QGKALADIQF AYLGDARNNV GNSLMVGAAK
MGMDIRLVGP QAYWPDEELV AACQAIAKQT GGKITLTENV AEGVQGCDFL YTDVWVSMGE
SPEAWDERVA LMKPYQVNMN VLKQTGNPNV KFMHCLPAFH NDETTIGKQV ADKFGMKGLE
VTEEVFESEH SIVFDEAENR MHTIKAVMVA TLGS
