OTC_COCIM
ID OTC_COCIM Reviewed; 349 AA.
AC P0CL21; J3KCR4; J3KD67;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Ornithine carbamoyltransferase, mitochondrial;
DE EC=2.1.3.3;
DE AltName: Full=Ornithine transcarbamylase;
DE Short=OTCase;
DE Flags: Precursor;
GN ORFNames=CIMG_04084;
OS Coccidioides immitis (strain RS) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=246410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RS;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=RS;
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-349.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of a mitochondrial ornithine carbamoyltransferase from
RT coccidioides immitis.";
RL Submitted (JUN-2011) to the PDB data bank.
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 -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAS33060.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GG704916; EAS33060.3; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_001244643.2; XM_001244642.2.
DR PDB; 3SDS; X-ray; 2.80 A; A/B/C=1-349.
DR PDBsum; 3SDS; -.
DR AlphaFoldDB; P0CL21; -.
DR SMR; P0CL21; -.
DR STRING; 246410.P0CL21; -.
DR EnsemblFungi; EAS33060; EAS33060; CIMG_04084.
DR GeneID; 4562518; -.
DR KEGG; cim:CIMG_04084; -.
DR InParanoid; P0CL21; -.
DR OrthoDB; 1404554at2759; -.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000001261; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; 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.
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;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..349
FT /note="Ornithine carbamoyltransferase, mitochondrial"
FT /id="PRO_0000405775"
FT ACT_SITE 303
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 73..76
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 124
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 151
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 154
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 195
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 261
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 265
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 266
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 303..304
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT BINDING 330
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000250|UniProtKB:P00480"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 30..47
FT /evidence="ECO:0007829|PDB:3SDS"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3SDS"
FT TURN 57..62
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3SDS"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 195..206
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:3SDS"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:3SDS"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 286..292
FT /evidence="ECO:0007829|PDB:3SDS"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:3SDS"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:3SDS"
FT HELIX 323..341
FT /evidence="ECO:0007829|PDB:3SDS"
SQ SEQUENCE 349 AA; 37999 MW; C9E68274B72900AE CRC64;
MAKNQWRPYT NGSHAPSTPR HLLSIADLTP TEFATLVRNA SSYKKTIKSD SMPERLTGAL
SGKTVAMMFS KRSTRTRVST EGAVVKMGGH PMFLGKDDIQ LGVNESLYDT SVVISSMVSC
IVARVGPHSD IANLAKHSSV PVINALCDTF HPLQAIADFL TIHESFASQS ATHGTHPSSL
GLEGLKIAWV GDANNVLFDL AIAATKMGVN VAVATPRGYE IPSHIVELIQ KAREGVQSPG
NLTQTTVPEV AVKDADVIVT DTWISMGQET EKIKRLEAFK DFKVTSELAK RGGAKENWKF
MHCLPRHPEE VSDEVFYSER SLVFPEAENR LWAAISALEA FVVNKGKIA
