ID   OTCC_OENOE              Reviewed;         351 AA.
AC   Q8VW55;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ornithine carbamoyltransferase, catabolic;
DE            Short=OTCase;
DE            EC=2.1.3.3;
GN   Name=arcB;
OS   Oenococcus oeni (Leuconostoc oenos).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=1247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 23279 / DSM 20252 / BCRC 14062 / CIP 106144 / JCM 6125 / NBRC
RC   100497 / NCDO 1674 / NCIMB 11648 / NRRL B-3472;
RX   PubMed=11605985; DOI=10.1016/s0923-2508(01)01244-x;
RA   Tonon T., Bourdineaud J.P., Lonvaud-Funel A.;
RT   "The arcABC gene cluster encoding the arginine deiminase pathway of
RT   Oenococcus oeni, and arginine induction of a CRP-like gene.";
RL   Res. Microbiol. 152:653-661(2001).
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; AF124851; AAL33871.1; -; Genomic_DNA.
DR   RefSeq; WP_002820808.1; NZ_SNSU01000001.1.
DR   AlphaFoldDB; Q8VW55; -.
DR   SMR; Q8VW55; -.
DR   PATRIC; fig|1247.145.peg.483; -.
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..351
FT                   /note="Ornithine carbamoyltransferase, catabolic"
FT                   /id="PRO_0000112976"
FT   BINDING         70..73
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         97
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         121
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         148..151
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         180
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         244
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         248..249
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         286..287
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         331
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   351 AA;  39789 MW;  FB610D09BCADB32D CRC64;
     MEQKLGNLVK KNVVNSVFQG RSLLAEKDFT PMELEYLIDF ALHLKALKKL GISHRYLEGK
     NIALLFEKTS TRTRSAFTTA SIDLGAHPEF LGSNDIQLGK KESVEDTARV LGSMFDGIEF
     RGFKQSVVDD LARYSGVPVW NGLTDEWHPT QMLADFMTIK ENFGHIKNIN LSYMGDGRNN
     TANSLLITGS MLGANIRIVS PKELQPSEKT TELAKKFAEK SGSRFLITDN IDEGVSKTNV
     LYTDVWVSMG ESDWEDRVKL LKPYQVNMET IRKTSTPDDQ LIFMHCLPAF HDINTDYGHE
     IFEKYGIKEM EVTDEVFRSI YARQFEEAEN RMHSIKAIMA ATLGNLFIPH V