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 27-MAR-2024, entry version 121. 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}; GN OrderedLocusNames=gll3101; OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421). OC Bacteria; Cyanobacteriota; Cyanophyceae; 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.gene:10760606; -. 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 OrthoDB; 9802587at2; -. 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; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00658; orni_carb_tr; 1. DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00102; OTCASE. DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 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 //