OTCC_STRE9
ID OTCC_STRE9 Reviewed; 337 AA.
AC Q8GG79; B9WVS9; Q301C2;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Ornithine carbamoyltransferase, catabolic {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=arcB {ECO:0000255|HAMAP-Rule:MF_01109}; ORFNames=SsuiDRAFT_2842;
OS Streptococcus suis (strain 89/1591).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286604;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=I9841/1;
RX PubMed=12446626; DOI=10.1128/jb.184.24.6768-6776.2002;
RA Winterhoff N., Goethe R., Gruening P., Valentin-Weigand P.;
RT "Identification and characterization of two temperature-induced surface-
RT associated proteins of Streptococcus suis with high homologies to members
RT of the arginine deiminase system of Streptococcus pyogenes.";
RL J. Bacteriol. 184:6768-6776(2002).
RN [2]
RP SEQUENCE REVISION TO 163; 187 AND 292.
RA Gruening P., Fulde M., Goethe R., Valentin-Weigand P., Winterhoff N.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=89/1591;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Chertkov O., Brettin T., Han C., Detter J.C., Gottschalk M., Richardson P.;
RT "Sequencing of the draft genome and assembly of Streptococcus suis
RT 89/1591.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01109};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC {ECO:0000255|HAMAP-Rule:MF_01109}.
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}.
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DR EMBL; AF546864; AAN76308.2; -; Genomic_DNA.
DR EMBL; AAFA03000016; EEF64413.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GG79; -.
DR SMR; Q8GG79; -.
DR GeneID; 8154075; -.
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..337
FT /note="Ornithine carbamoyltransferase, catabolic"
FT /id="PRO_0000113043"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 167
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 231
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 235..236
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 203
FT /note="G -> V (in Ref. 3; EEF64413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 37856 MW; C5E42EFCAFC3EC47 CRC64;
MTNVFKGRHF LAEKDFTRAE LEWLIDFSAH LKDLKKRNIP HRYLEGKNIA LLFEKTSTRT
RAAFTVASID LGAHPEYLGA NDIQLGKKES TEDTAKVLGR MFDGIEFRGF SQKMVEELAE
FSGVPVWNGL TDAWHPTQML ADYLTVKENF GKLEGLTLVY CGDGRNNVAN SLLVTGAILG
VNVHIFSPKE LFPEEEVVAL AEGFAKESGA RVLITDNADE AVKGADVLYT DVWVSMGEED
KFAERVALLK PYQVNMELVK KAENENLIFL HCLPAFHDTN TVYGKDVAEK FGVEEMEVTD
EVFRSKYARH FDQAENRMHT IKAVMAATLG DPFVPRV
