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OTC_CERSK
ID   OTC_CERSK               Reviewed;         308 AA.
AC   B9KMW0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Ornithine carbamoyltransferase {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};
GN   OrderedLocusNames=RSKD131_0312;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(2009).
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; CP001150; ACM00172.1; -; Genomic_DNA.
DR   RefSeq; WP_012643626.1; NC_011963.1.
DR   AlphaFoldDB; B9KMW0; -.
DR   SMR; B9KMW0; -.
DR   EnsemblBacteria; ACM00172; ACM00172; RSKD131_0312.
DR   GeneID; 67445790; -.
DR   KEGG; rsk:RSKD131_0312; -.
DR   HOGENOM; CLU_043846_3_2_5; -.
DR   OMA; DGNNVCN; -.
DR   UniPathway; UPA00254; UER00365.
DR   Proteomes; UP000001597; Chromosome 1.
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; Transferase.
FT   CHAIN           1..308
FT                   /note="Ornithine carbamoyltransferase"
FT                   /id="PRO_1000163979"
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         165
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         225
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         229..230
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         266..267
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         294
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ   SEQUENCE   308 AA;  34322 MW;  BC9EDE5886B51F4F CRC64;
     MNHFLDIHKT DTAELRQMMD SAHAMKAARK GRPKGQFDED QPLAGRMVAL IFEKPSTRTR
     VSFDVGVRQM GGQTMVLSGK EMQLGHGETI ADTARVLSRY VDLIMIRTFE EATLLEMAEH
     ATVPVINGLT NRTHPCQIMA DVMTYEEHRG PIAGRKVVWA GDGNNVCASF LHAAGQFGFD
     FTFTGPPTLD PEAEFVGYAR EKGRRVSIER DPAKAVAGAD LVVTDTWVSM HDPQSARERR
     HNQLRPYQVN EALMAQAKPD ALFMHCLPAH RDDEATSAVM DGPHSVIFDE AENRLHAQKA
     IMRWCLGL
 
 
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