ID OTCC2_STRA5 Reviewed; 337 AA. AC P65606; Q8DWQ0; Q8E2J8; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 119. DE RecName: Full=Ornithine carbamoyltransferase 2, catabolic; DE Short=OTCase 2; DE EC=2.1.3.3; GN Name=arcB2; OrderedLocusNames=SAG2165; OS Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=208435; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-611 / 2603 V/R; RX PubMed=12200547; DOI=10.1073/pnas.182380799; RA Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N., RA Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D., RA Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C., RA DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D., RA Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A., RA Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T., RA Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D., RA Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.; RT "Complete genome sequence and comparative genomic analysis of an emerging RT human pathogen, serotype V Streptococcus agalactiae."; RL Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(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 = L-citrulline + phosphate + CC H(+); Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE009948; AAN01023.1; -; Genomic_DNA. DR RefSeq; WP_000195397.1; NC_004116.1. DR AlphaFoldDB; P65606; -. DR SMR; P65606; -. DR STRING; 208435.SAG2165; -. DR PaxDb; 208435-SAG2165; -. DR KEGG; sag:SAG2165; -. DR PATRIC; fig|208435.3.peg.2168; -. DR HOGENOM; CLU_043846_3_1_9; -. DR OrthoDB; 9802587at2; -. DR UniPathway; UPA00254; UER00365. DR Proteomes; UP000000821; 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:0006527; P:L-arginine catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0019240; P:L-citrulline biosynthetic process; IEA:UniProtKB-ARBA. DR FunFam; 3.40.50.1370:FF:000004; Ornithine carbamoyltransferase; 1. DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 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 NCBIfam; TIGR00658; orni_carb_tr; 1. DR NCBIfam; NF001986; PRK00779.1; 1. DR PANTHER; PTHR45753:SF1; ORNITHINE CARBAMOYLTRANSFERASE, CATABOLIC; 1. DR PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00102; OTCASE. DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 3: Inferred from homology; KW Arginine metabolism; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1..337 FT /note="Ornithine carbamoyltransferase 2, catabolic" FT /id="PRO_0000113028" 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" SQ SEQUENCE 337 AA; 38119 MW; 420ADF4225E1CE64 CRC64; MTQVFQGRSF LAEKDFSREE FEYLIDFSAH LKDLKKRGVP HHYLEGKNIA LLFEKTSTRT RAAFTTAAID LGAHPEYLGA NDIQLGKKES TEDTAKVLGR MFDGIEFRGF SQRMVEELAE FSGVPVWNGL TDEWHPTQML ADYLTIKENF GKLEGITLVY CGDGRNNVAN SLLVAGTLMG VNVHIFSPKE LFPAEEIVKL AEEYAKESGA HVLVTDNVDE AVKGADVFYT DVWVSMGEED KFKERVELLQ PYQVNMELIK KANNDNLIFL HCLPAFHDTN TVYGKDVAEK FGVKEMEVTD EVFRSKYARH FDQAENRMHT IKAVMAATLG NLFIPKV //