ID   OTCC_BORAF              Reviewed;         328 AA.
AC   O51897;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, 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;
OS   Borreliella afzelii (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=29518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R-IP3;
RX   PubMed=9402027; DOI=10.1046/j.1365-2958.1997.6051963.x;
RA   Casjens S., Murphy M., DeLange M., Sampson L., van Vugt R., Huang W.M.;
RT   "Telomeres of the linear chromosomes of Lyme disease spirochaetes:
RT   nucleotide sequence and possible exchange with linear plasmid telomeres.";
RL   Mol. Microbiol. 26:581-596(1997).
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; AF008219; AAB93999.1; -; Genomic_DNA.
DR   RefSeq; WP_011601269.1; NZ_JACHGM010000001.1.
DR   AlphaFoldDB; O51897; -.
DR   SMR; O51897; -.
DR   OMA; DGNNVCN; -.
DR   UniPathway; UPA00254; UER00365.
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   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; Transferase.
FT   CHAIN           1..328
FT                   /note="Ornithine carbamoyltransferase, catabolic"
FT                   /id="PRO_0000112888"
FT   BINDING         56..59
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         83
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         107
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         134..137
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         270..271
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         315
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   328 AA;  36561 MW;  EC7F89DFCD3547AD CRC64;
     MYNLRNRSFL NLLDFTSKDI KYLLDLSIDL KKSKYAGIEV QKLKGKNIVI IFEKDSTRTR
     CAFEIAAYDQ GANITYLGPK GNQIGVKESM KDTARVLGRM YDAIGFRGFS QETVECLANY
     SNVPVYNGLT DISHPTQILA DLMTIKEHKG SLKGIKIVFC GDGRGNIANS LLKGCAIMGL
     DFRIFAPKEL FPDSNLTLKA KSLALKSGGK ITITDSKEEA VKCADVVYTD VWVSMGEESN
     WEDRINLLKL YQVNKELMCM AKDDAIFMHC LPAFHDLSTV VGRDIFDKYG LDGIEVTEEI
     FESKNSVVFD VAENRVHAIK AVMVSTLG