OTCC_CLOPE
ID OTCC_CLOPE Reviewed; 331 AA.
AC P0C2E4; Q46169; Q46255;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ornithine carbamoyltransferase, catabolic;
DE Short=OTCase;
DE EC=2.1.3.3;
GN Name=arcB; OrderedLocusNames=CPE0169;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=9053381; DOI=10.1111/j.1574-6968.1997.tb10186.x;
RA Ohtani K., Bando M., Swe T., Banu S., Oe M., Hayashi H., Shimizu T.;
RT "Collagenase gene (colA) is located in the 3'-flanking region of the
RT perfringolysin O (pfoA) locus in Clostridium perfringens.";
RL FEMS Microbiol. Lett. 146:155-159(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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 degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 2/2.
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; X97768; CAA66365.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB79875.1; -; Genomic_DNA.
DR RefSeq; WP_003462779.1; NC_003366.1.
DR AlphaFoldDB; P0C2E4; -.
DR SMR; P0C2E4; -.
DR STRING; 195102.gene:10489413; -.
DR PRIDE; P0C2E4; -.
DR EnsemblBacteria; BAB79875; BAB79875; BAB79875.
DR GeneID; 29572716; -.
DR KEGG; cpe:CPE0169; -.
DR HOGENOM; CLU_043846_3_1_9; -.
DR OMA; NPEVIFM; -.
DR UniPathway; UPA00254; UER00365.
DR Proteomes; UP000000818; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019546; P:arginine deiminase pathway; 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 3: Inferred from homology;
KW Arginine metabolism; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..331
FT /note="Ornithine carbamoyltransferase, catabolic"
FT /id="PRO_0000112911"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 82
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 106
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 133..136
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 166
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 230
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 234..235
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 272..273
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 317
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT CONFLICT 154
FT /note="E -> A (in Ref. 1; CAA66365)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="D -> H (in Ref. 1; CAA66365)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..290
FT /note="MMDR -> RWID (in Ref. 1; CAA66365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 37153 MW; 1AAC566B48DB4180 CRC64;
MAVNLKGRSF LTLKDFTPAE IRYLLDLSHD LKAKKRAGIL GDSLKGKNVV LLFEKTSTRT
RCAFECGAAE EGAHVTFLTN SQMGKKESIE DTAKVLGRMY DGIEFRGFKQ STVEELAKHA
GVPVWNGLTD ADHPTQILAD FLTIEEHAHK PLSEIKLVFT GDTRNNMSYA LMYGAAKMGM
HFVALGPDSL KPDEDILKEM QEYSKETGAT IEFSSNVDEA VKGADVIYTD IWVSMGEDES
LYPERVKLLT PYKVTREMMN KTGNKNTLFM HCLPSFHDED TEVCKDMMDR LGLDIREVED
EVFRSKNSVV FDEAENRMHT IKAVMVATAG R
