OTC_GLOVI
ID OTC_GLOVI Reviewed; 313 AA.
AC Q7NGR7;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=gll3101;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), AND SUBUNIT.
RG New york sgx research center for structural genomics (NYSGXRC);
RA Fedorov A.A., Fedorov E.V., Toro R., Ramagopal U.A., Sauder J.M.,
RA Burley S.K., Almo S.C.;
RT "Crystal structure of ornithine carbamoyltransferase from Gloeobacter
RT violaceus.";
RL Submitted (FEB-2009) 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: Homohexamer. {ECO:0000305|Ref.2}.
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; BA000045; BAC91042.1; -; Genomic_DNA.
DR RefSeq; NP_926047.1; NC_005125.1.
DR RefSeq; WP_011143094.1; NC_005125.1.
DR PDB; 3GD5; X-ray; 2.10 A; A/B/C/D/E/F=2-313.
DR PDBsum; 3GD5; -.
DR AlphaFoldDB; Q7NGR7; -.
DR SMR; Q7NGR7; -.
DR STRING; 251221.35213672; -.
DR EnsemblBacteria; BAC91042; BAC91042; BAC91042.
DR KEGG; gvi:gll3101; -.
DR PATRIC; fig|251221.4.peg.3130; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_2_3; -.
DR InParanoid; Q7NGR7; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 988597at2; -.
DR PhylomeDB; Q7NGR7; -.
DR UniPathway; UPA00068; UER00112.
DR EvolutionaryTrace; Q7NGR7; -.
DR Proteomes; UP000000557; 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; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
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 Reference proteome; Transferase.
FT CHAIN 1..313
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000112927"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 166
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 230
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 234..235
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 270..271
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT BINDING 298
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P04391"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3GD5"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:3GD5"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:3GD5"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:3GD5"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 112..122
FT /evidence="ECO:0007829|PDB:3GD5"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:3GD5"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:3GD5"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:3GD5"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:3GD5"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 245..248
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 255..259
FT /evidence="ECO:0007829|PDB:3GD5"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3GD5"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:3GD5"
FT HELIX 291..310
FT /evidence="ECO:0007829|PDB:3GD5"
SQ SEQUENCE 313 AA; 33958 MW; 705948D76BE67854 CRC64;
MSASLGATRF RPDLLSLDDL DEAQLHALLT LAHQLKRGER VANLHGKVLG LVFLKASTRT
RVSFTVAMYQ LGGQVIDLSP SNTQVGRGEP VRDTARVLGR YVDGLAIRTF AQTELEEYAH
YAGIPVINAL TDHEHPCQVV ADLLTIRENF GRLAGLKLAY VGDGNNVAHS LLLGCAKVGM
SIAVATPEGF TPDPAVSARA SEIAGRTGAE VQILRDPFEA ARGAHILYTD VWTSMGQEAE
TQHRLQLFEQ YQINAALLNC AAAEAIVLHC LPAHRGEEIT DEVMEGPRSR IWDEAENRLH
AQKAVLAALM GGR
